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- PDB-5sy5: Crystal Structure of the Heterodimeric NPAS1-ARNT Complex -

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Basic information

Entry
Database: PDB / ID: 5sy5
TitleCrystal Structure of the Heterodimeric NPAS1-ARNT Complex
Components
  • Aryl hydrocarbon receptor nuclear translocator
  • Neuronal PAS domain-containing protein 1
KeywordsTRANSCRIPTION / bHLH-PAS protein / transcription factor / heterodimeric complex
Function / homology
Function and homology information


Xenobiotics / Aryl hydrocarbon receptor signalling / Phase I - Functionalization of compounds / NPAS4 regulates expression of target genes / Regulation of gene expression by Hypoxia-inducible Factor / Endogenous sterols / nuclear aryl hydrocarbon receptor complex / positive regulation of hormone biosynthetic process / positive regulation of protein sumoylation / maternal behavior ...Xenobiotics / Aryl hydrocarbon receptor signalling / Phase I - Functionalization of compounds / NPAS4 regulates expression of target genes / Regulation of gene expression by Hypoxia-inducible Factor / Endogenous sterols / nuclear aryl hydrocarbon receptor complex / positive regulation of hormone biosynthetic process / positive regulation of protein sumoylation / maternal behavior / startle response / aryl hydrocarbon receptor binding / positive regulation of vascular endothelial growth factor production / embryonic placenta development / cis-regulatory region sequence-specific DNA binding / positive regulation of glycolytic process / RNA polymerase II transcription regulatory region sequence-specific DNA binding / response to toxic substance / negative regulation of inflammatory response / RNA polymerase II transcription regulator complex / nuclear receptor activity / sequence-specific double-stranded DNA binding / cellular response to oxidative stress / transcription regulator complex / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / cell differentiation / response to hypoxia / nuclear body / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / protein heterodimerization activity / negative regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / nucleus / cytoplasm
Similarity search - Function
: / Nuclear translocator / PAS fold-3 / PAS fold / Helix-loop-helix DNA-binding domain / PAC motif / Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) / PAS domain / helix loop helix domain / Myc-type, basic helix-loop-helix (bHLH) domain ...: / Nuclear translocator / PAS fold-3 / PAS fold / Helix-loop-helix DNA-binding domain / PAC motif / Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) / PAS domain / helix loop helix domain / Myc-type, basic helix-loop-helix (bHLH) domain / Myc-type, basic helix-loop-helix (bHLH) domain profile. / Helix-loop-helix DNA-binding domain superfamily / PAS fold / PAS fold / PAS domain / PAS repeat profile. / PAS domain / PAS domain superfamily
Similarity search - Domain/homology
Aryl hydrocarbon receptor nuclear translocator / Neuronal PAS domain-containing protein 1
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.201 Å
AuthorsWu, D. / Su, X. / Potluri, N. / Kim, Y. / Rastinejad, F.
CitationJournal: Elife / Year: 2016
Title: NPAS1-ARNT and NPAS3-ARNT crystal structures implicate the bHLH-PAS family as multi-ligand binding transcription factors.
Authors: Wu, D. / Su, X. / Potluri, N. / Kim, Y. / Rastinejad, F.
History
DepositionAug 10, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 9, 2016Provider: repository / Type: Initial release
Revision 1.1Oct 4, 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 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Aryl hydrocarbon receptor nuclear translocator
B: Neuronal PAS domain-containing protein 1
C: Aryl hydrocarbon receptor nuclear translocator
D: Neuronal PAS domain-containing protein 1
E: Aryl hydrocarbon receptor nuclear translocator
F: Neuronal PAS domain-containing protein 1


Theoretical massNumber of molelcules
Total (without water)258,2916
Polymers258,2916
Non-polymers00
Water00
1
A: Aryl hydrocarbon receptor nuclear translocator
B: Neuronal PAS domain-containing protein 1


Theoretical massNumber of molelcules
Total (without water)86,0972
Polymers86,0972
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8160 Å2
ΔGint-54 kcal/mol
Surface area25000 Å2
MethodPISA
2
C: Aryl hydrocarbon receptor nuclear translocator
D: Neuronal PAS domain-containing protein 1


Theoretical massNumber of molelcules
Total (without water)86,0972
Polymers86,0972
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8440 Å2
ΔGint-59 kcal/mol
Surface area24660 Å2
MethodPISA
3
E: Aryl hydrocarbon receptor nuclear translocator
F: Neuronal PAS domain-containing protein 1


Theoretical massNumber of molelcules
Total (without water)86,0972
Polymers86,0972
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8940 Å2
ΔGint-60 kcal/mol
Surface area25260 Å2
MethodPISA
4


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area26840 Å2
ΔGint-173 kcal/mol
Surface area73610 Å2
MethodPISA
Unit cell
Length a, b, c (Å)69.948, 81.187, 138.062
Angle α, β, γ (deg.)90.380, 95.080, 107.390
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain B and (resseq 52:65 or resseq 67:80 or resseq...
21(chain D and (resseq 52:65 or resseq 67:80 or resseq...
31(chain F and (resseq 52:65 or resseq 67:80 or resseq...
12(chain A and (resseq 103 or resseq 105:123 or resseq...
22(chain C and (resseq 103 or resseq 105:123 or resseq...
32(chain E and (resseq 103 or resseq 105:123 or resseq...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ASNASNPHEPHE(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB52 - 6512 - 25
121GLUGLUSERSER(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB67 - 8027 - 40
131LEULEUARGARG(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB82 - 9842 - 58
141PHEPHEGLYGLY(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB100 - 10960 - 69
151GLYGLYASPASP(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB139 - 18499 - 144
161TYRTYRTYRTYR(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB185145
171ASNASNPROPRO(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB52 - 42212 - 382
181ASNASNPROPRO(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB52 - 42212 - 382
191ASNASNPROPRO(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB52 - 42212 - 382
1101ASNASNPROPRO(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB52 - 42212 - 382
1111ASNASNPROPRO(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB52 - 42212 - 382
1121ASNASNPROPRO(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB52 - 42212 - 382
1131ASNASNPROPRO(chain B and (resseq 52:65 or resseq 67:80 or resseq...BB52 - 42212 - 382
211ASNASNPHEPHE(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD52 - 6512 - 25
221GLUGLUSERSER(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD67 - 8027 - 40
231LEULEUARGARG(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD82 - 9842 - 58
241PHEPHEGLYGLY(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD100 - 10960 - 69
251GLYGLYASPASP(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD139 - 18499 - 144
261TYRTYRTYRTYR(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD185145
271ASNASNLEULEU(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD52 - 42112 - 381
281ASNASNLEULEU(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD52 - 42112 - 381
291ASNASNLEULEU(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD52 - 42112 - 381
2101ASNASNLEULEU(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD52 - 42112 - 381
2111ASNASNLEULEU(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD52 - 42112 - 381
2121ASNASNLEULEU(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD52 - 42112 - 381
2131ASNASNLEULEU(chain D and (resseq 52:65 or resseq 67:80 or resseq...DD52 - 42112 - 381
311ASNASNPHEPHE(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF52 - 6512 - 25
321GLUGLUSERSER(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF67 - 8027 - 40
331LEULEUARGARG(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF82 - 9842 - 58
341PHEPHEGLYGLY(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF100 - 10960 - 69
351GLYGLYASPASP(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF139 - 18499 - 144
361TYRTYRTYRTYR(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF185145
371ARGARGLEULEU(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF51 - 42111 - 381
381ARGARGLEULEU(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF51 - 42111 - 381
391ARGARGLEULEU(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF51 - 42111 - 381
3101ARGARGLEULEU(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF51 - 42111 - 381
3111ARGARGLEULEU(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF51 - 42111 - 381
3121ARGARGLEULEU(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF51 - 42111 - 381
3131ARGARGLEULEU(chain F and (resseq 52:65 or resseq 67:80 or resseq...FF51 - 42111 - 381
112ASNASNASNASN(chain A and (resseq 103 or resseq 105:123 or resseq...AA10323
122METMETALAALA(chain A and (resseq 103 or resseq 105:123 or resseq...AA105 - 12325 - 43
132PROPROLEULEU(chain A and (resseq 103 or resseq 105:123 or resseq...AA126 - 14246 - 62
142SERSERCYSCYS(chain A and (resseq 103 or resseq 105:123 or resseq...AA157 - 18177 - 101
152THRTHRGLYGLY(chain A and (resseq 103 or resseq 105:123 or resseq...AA183 - 184103 - 104
162VALVALVALVAL(chain A and (resseq 103 or resseq 105:123 or resseq...AA186 - 187106 - 107
172TYRTYRTYRTYR(chain A and (resseq 103 or resseq 105:123 or resseq...AA188108
182ARGARGVALVAL(chain A and (resseq 103 or resseq 105:123 or resseq...AA99 - 46419 - 384
192ARGARGVALVAL(chain A and (resseq 103 or resseq 105:123 or resseq...AA99 - 46419 - 384
1102ARGARGVALVAL(chain A and (resseq 103 or resseq 105:123 or resseq...AA99 - 46419 - 384
1112ARGARGVALVAL(chain A and (resseq 103 or resseq 105:123 or resseq...AA99 - 46419 - 384
1122ARGARGVALVAL(chain A and (resseq 103 or resseq 105:123 or resseq...AA99 - 46419 - 384
1132ARGARGVALVAL(chain A and (resseq 103 or resseq 105:123 or resseq...AA99 - 46419 - 384
1142ARGARGVALVAL(chain A and (resseq 103 or resseq 105:123 or resseq...AA99 - 46419 - 384
212ASNASNASNASN(chain C and (resseq 103 or resseq 105:123 or resseq...CC10323
222METMETALAALA(chain C and (resseq 103 or resseq 105:123 or resseq...CC105 - 12325 - 43
232PROPROLEULEU(chain C and (resseq 103 or resseq 105:123 or resseq...CC126 - 14246 - 62
242SERSERCYSCYS(chain C and (resseq 103 or resseq 105:123 or resseq...CC157 - 18177 - 101
252THRTHRGLYGLY(chain C and (resseq 103 or resseq 105:123 or resseq...CC183 - 184103 - 104
262VALVALVALVAL(chain C and (resseq 103 or resseq 105:123 or resseq...CC186 - 187106 - 107
272TYRTYRTYRTYR(chain C and (resseq 103 or resseq 105:123 or resseq...CC188108
282ASNASNVALVAL(chain C and (resseq 103 or resseq 105:123 or resseq...CC103 - 46423 - 384
292ASNASNVALVAL(chain C and (resseq 103 or resseq 105:123 or resseq...CC103 - 46423 - 384
2102ASNASNVALVAL(chain C and (resseq 103 or resseq 105:123 or resseq...CC103 - 46423 - 384
2112ASNASNVALVAL(chain C and (resseq 103 or resseq 105:123 or resseq...CC103 - 46423 - 384
2122ASNASNVALVAL(chain C and (resseq 103 or resseq 105:123 or resseq...CC103 - 46423 - 384
2132ASNASNVALVAL(chain C and (resseq 103 or resseq 105:123 or resseq...CC103 - 46423 - 384
2142ASNASNVALVAL(chain C and (resseq 103 or resseq 105:123 or resseq...CC103 - 46423 - 384
312ASNASNASNASN(chain E and (resseq 103 or resseq 105:123 or resseq...EE10323
322METMETALAALA(chain E and (resseq 103 or resseq 105:123 or resseq...EE105 - 12325 - 43
332PROPROLEULEU(chain E and (resseq 103 or resseq 105:123 or resseq...EE126 - 14246 - 62
342SERSERCYSCYS(chain E and (resseq 103 or resseq 105:123 or resseq...EE157 - 18177 - 101
352THRTHRGLYGLY(chain E and (resseq 103 or resseq 105:123 or resseq...EE183 - 184103 - 104
362VALVALVALVAL(chain E and (resseq 103 or resseq 105:123 or resseq...EE186 - 187106 - 107
372TYRTYRTYRTYR(chain E and (resseq 103 or resseq 105:123 or resseq...EE188108
382GLUGLUVALVAL(chain E and (resseq 103 or resseq 105:123 or resseq...EE98 - 46418 - 384
392GLUGLUVALVAL(chain E and (resseq 103 or resseq 105:123 or resseq...EE98 - 46418 - 384
3102GLUGLUVALVAL(chain E and (resseq 103 or resseq 105:123 or resseq...EE98 - 46418 - 384
3112GLUGLUVALVAL(chain E and (resseq 103 or resseq 105:123 or resseq...EE98 - 46418 - 384
3122GLUGLUVALVAL(chain E and (resseq 103 or resseq 105:123 or resseq...EE98 - 46418 - 384
3132GLUGLUVALVAL(chain E and (resseq 103 or resseq 105:123 or resseq...EE98 - 46418 - 384
3142GLUGLUVALVAL(chain E and (resseq 103 or resseq 105:123 or resseq...EE98 - 46418 - 384

NCS ensembles :
ID
1
2

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Components

#1: Protein Aryl hydrocarbon receptor nuclear translocator / ARNT protein / Dioxin receptor / nuclear translocator / Hypoxia-inducible factor 1-beta / HIF1-beta


Mass: 43437.391 Da / Num. of mol.: 3 / Fragment: unp residues 82-464
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Arnt / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P53762
#2: Protein Neuronal PAS domain-containing protein 1 / Neuronal PAS1


Mass: 42659.609 Da / Num. of mol.: 3 / Fragment: unp reisdues 43-423
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Npas1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P97459

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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: 2.88 Å3/Da / Density % sol: 57.35 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 2% Tacsimate pH 7.0, 3% PEG3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.979 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 24, 2013
RadiationMonochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 3.2→50 Å / Num. obs: 46508 / % possible obs: 98.6 % / Redundancy: 2.1 % / Biso Wilson estimate: 55.76 Å2 / Rmerge(I) obs: 0.055 / Net I/av σ(I): 13.96 / Net I/σ(I): 9.5
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsCC1/2Diffraction-ID% possible all
3.2-3.262.20.7640.459198.3
3.26-3.312.20.6820.47198.7
3.31-3.382.20.5480.633198.5
3.38-3.452.20.4260.716198.6
3.45-3.522.20.3470.791199.1
3.52-3.62.20.2870.823198.9
3.6-3.692.20.2010.889198.9
3.69-3.792.20.1690.928198.8
3.79-3.912.20.1390.948198.9
3.91-4.032.20.1070.97199
4.03-4.182.20.0780.979198.9
4.18-4.342.20.0590.985198.8
4.34-4.542.20.0480.989198.5
4.54-4.782.20.0410.991198.7
4.78-5.082.10.040.991199
5.08-5.472.10.040.991198.8
5.47-6.022.10.0420.988199
6.02-6.892.10.0350.992198.8
6.89-8.6720.0250.994199.2
8.67-502.10.0260.993194.6

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
HKL-3000data collection
HKL-3000data scaling
PHASERphasing
PHENIX1.10.1_2155refinement
PDB_EXTRACT3.2data extraction
HKL-3000data reduction
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4ZP4

4zp4


Resolution: 3.201→38.926 Å / SU ML: 0.37 / Cross valid method: FREE R-VALUE / σ(F): 1.98 / Phase error: 25.26
RfactorNum. reflection% reflection
Rfree0.2467 1999 5.11 %
Rwork0.1764 --
obs0.18 39086 82.28 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 138.22 Å2 / Biso mean: 49.5499 Å2 / Biso min: 17.26 Å2
Refinement stepCycle: final / Resolution: 3.201→38.926 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13303 0 0 0 13303
Num. residues----1669
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01113595
X-RAY DIFFRACTIONf_angle_d1.36118351
X-RAY DIFFRACTIONf_chiral_restr0.0692063
X-RAY DIFFRACTIONf_plane_restr0.0082316
X-RAY DIFFRACTIONf_dihedral_angle_d12.668043
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11B3575X-RAY DIFFRACTION11.415TORSIONAL
12D3575X-RAY DIFFRACTION11.415TORSIONAL
13F3575X-RAY DIFFRACTION11.415TORSIONAL
21A3418X-RAY DIFFRACTION11.415TORSIONAL
22C3418X-RAY DIFFRACTION11.415TORSIONAL
23E3418X-RAY DIFFRACTION11.415TORSIONAL
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 (%)
3.2013-3.28130.4396280.290739942713
3.2813-3.370.3434670.26671144121136
3.37-3.46910.376870.24681812189956
3.4691-3.5810.31511270.23262317244473
3.581-3.70890.3071460.21022904305089
3.7089-3.85730.25521880.1983126331498
3.8573-4.03270.2771750.18463172334799
4.0327-4.2450.2331780.163195337399
4.245-4.51060.21971680.14113165333399
4.5106-4.85830.19731830.13383171335499
4.8583-5.34610.20431640.14273214337899
5.3461-6.11710.2131640.18093170333499
6.1171-7.69710.28181640.19443194335899
7.6971-38.92920.21921600.1733104326496
Refinement TLS params.Method: refined / Origin x: 64.9028 Å / Origin y: 64.8778 Å / Origin z: -17.696 Å
111213212223313233
T0.1896 Å2-0.0238 Å20.0165 Å2-0.2478 Å20.0069 Å2--0.2629 Å2
L0.0173 °2-0.0582 °2-0.0104 °2-0.2221 °20.0443 °2--0.5454 °2
S0.014 Å °-0.0005 Å °-0.017 Å °0.084 Å °-0.0267 Å °0.0148 Å °0.0958 Å °-0.0053 Å °0.0132 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1allA99 - 464
2X-RAY DIFFRACTION1allB52 - 422
3X-RAY DIFFRACTION1allC103 - 464
4X-RAY DIFFRACTION1allD52 - 421
5X-RAY DIFFRACTION1allE98 - 464
6X-RAY DIFFRACTION1allF51 - 421

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