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- PDB-7xvl: Crystal Structure of Nucleosome-H1.0 Linker Histone Assembly (sti... -

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Entry
Database: PDB / ID: 7xvl
TitleCrystal Structure of Nucleosome-H1.0 Linker Histone Assembly (sticky-169an DNA fragment)
Components
  • (DNA (169-MER)) x 2
  • Histone H1.0
  • Histone H2A type 1-B/E
  • Histone H2B type 1-J
  • Histone H3.1Histone H3
  • Histone H4
KeywordsDNA BINDING PROTEIN/DNA / linker histone / nucleosome binding / chromatin structure / chromatin compaction / histone variants / STRUCTURAL PROTEIN-DNA complex / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex
Function / homology
Function and homology information


negative regulation of DNA recombination / positive regulation of transcription regulatory region DNA binding / Apoptosis induced DNA fragmentation / chromosome condensation / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / heterochromatin organization / minor groove of adenine-thymine-rich DNA binding / nucleosomal DNA binding / negative regulation of tumor necrosis factor-mediated signaling pathway / negative regulation of megakaryocyte differentiation ...negative regulation of DNA recombination / positive regulation of transcription regulatory region DNA binding / Apoptosis induced DNA fragmentation / chromosome condensation / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / heterochromatin organization / minor groove of adenine-thymine-rich DNA binding / nucleosomal DNA binding / negative regulation of tumor necrosis factor-mediated signaling pathway / negative regulation of megakaryocyte differentiation / protein localization to CENP-A containing chromatin / Chromatin modifying enzymes / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / heterochromatin formation / epigenetic regulation of gene expression / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Deposition of new CENPA-containing nucleosomes at the centromere / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / Meiotic synapsis / transcription repressor complex / telomere organization / RNA Polymerase I Promoter Opening / Interleukin-7 signaling / Assembly of the ORC complex at the origin of replication / SUMOylation of chromatin organization proteins / DNA methylation / Condensation of Prophase Chromosomes / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / SIRT1 negatively regulates rRNA expression / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / innate immune response in mucosa / PRC2 methylates histones and DNA / Defective pyroptosis / HDACs deacetylate histones / RNA Polymerase I Promoter Escape / lipopolysaccharide binding / Nonhomologous End-Joining (NHEJ) / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / euchromatin / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / NoRC negatively regulates rRNA expression / HDMs demethylate histones / G2/M DNA damage checkpoint / B-WICH complex positively regulates rRNA expression / DNA Damage/Telomere Stress Induced Senescence / Metalloprotease DUBs / chromatin DNA binding / PKMTs methylate histone lysines / RMTs methylate histone arginines / Meiotic recombination / Pre-NOTCH Transcription and Translation / Activation of anterior HOX genes in hindbrain development during early embryogenesis / HCMV Early Events / Transcriptional regulation of granulopoiesis / structural constituent of chromatin / UCH proteinases / nucleosome / antimicrobial humoral immune response mediated by antimicrobial peptide / nucleosome assembly / actin cytoskeleton / E3 ubiquitin ligases ubiquitinate target proteins / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / RUNX1 regulates transcription of genes involved in differentiation of HSCs / gene expression / chromatin organization / Factors involved in megakaryocyte development and platelet production / HATs acetylate histones / Processing of DNA double-strand break ends / antibacterial humoral response / Senescence-Associated Secretory Phenotype (SASP) / double-stranded DNA binding / Oxidative Stress Induced Senescence / killing of cells of another organism / Estrogen-dependent gene expression / defense response to Gram-negative bacterium / chromosome, telomeric region / nuclear body / Ub-specific processing proteases / defense response to Gram-positive bacterium / cadherin binding / protein heterodimerization activity / Amyloid fiber formation / negative regulation of cell population proliferation / chromatin / Golgi apparatus / protein-containing complex / DNA binding / extracellular space / RNA binding / extracellular exosome / extracellular region / nucleoplasm
Similarity search - Function
Linker histone H1/H5 / linker histone H1 and H5 family / Linker histone H1/H5, domain H15 / Linker histone H1/H5 globular (H15) domain profile. / Domain in histone families 1 and 5 / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site / Histone H2A signature. ...Linker histone H1/H5 / linker histone H1 and H5 family / Linker histone H1/H5, domain H15 / Linker histone H1/H5 globular (H15) domain profile. / Domain in histone families 1 and 5 / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site / Histone H2A signature. / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone H2A / Histone 2A / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
DNA / DNA (> 10) / DNA (> 100) / Histone H2A type 1-B/E / Histone H2B type 1-J / Histone H1.0 / Histone H4 / Histone H3.1
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.506 Å
AuthorsAdhireksan, Z. / Qiuye, B. / Lee, P.L. / Sharma, D. / Padavattan, S. / Davey, C.A.
Funding support Singapore, 2items
OrganizationGrant numberCountry
Ministry of Education (MoE, Singapore)MOE2015-T2-2-089 Singapore
Ministry of Education (MoE, Singapore)MOE2012-T3-1-001 Singapore
CitationJournal: To Be Published
Title: Crystal Structure of Nucleosome-H1.0 Linker Histone Assembly (sticky-169an DNA fragment)
Authors: Adhireksan, Z. / Sharma, D. / Qiuye, B. / Lee, P.L. / Padavattan, S. / Davey, C.A.
History
DepositionMay 24, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 24, 2023Provider: repository / Type: Initial release
Revision 1.1Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 2.0Apr 3, 2024Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Other / Refinement description / Structure summary
Category: atom_site / atom_sites ...atom_site / atom_sites / citation / citation_author / ndb_struct_na_base_pair / pdbx_contact_author / pdbx_poly_seq_scheme / pdbx_struct_sheet_hbond / pdbx_unobs_or_zero_occ_residues / pdbx_validate_close_contact / pdbx_validate_rmsd_angle / pdbx_validate_rmsd_bond / pdbx_validate_symm_contact / pdbx_validate_torsion / refine / refine_hist / refine_ls_restr / refine_ls_shell / reflns / software / struct_conf / struct_conn / struct_sheet / struct_sheet_order / struct_sheet_range
Item: _atom_sites.fract_transf_matrix[2][1] / _atom_sites.fract_transf_matrix[3][2] ..._atom_sites.fract_transf_matrix[2][1] / _atom_sites.fract_transf_matrix[3][2] / _citation.title / _citation_author.identifier_ORCID / _citation_author.name / _ndb_struct_na_base_pair.buckle / _ndb_struct_na_base_pair.opening / _ndb_struct_na_base_pair.propeller / _ndb_struct_na_base_pair.shear / _ndb_struct_na_base_pair.stagger / _ndb_struct_na_base_pair.stretch / _pdbx_contact_author.address_1 / _pdbx_contact_author.address_2 / _pdbx_contact_author.city / _pdbx_contact_author.country / _pdbx_contact_author.email / _pdbx_contact_author.id / _pdbx_contact_author.phone / _pdbx_contact_author.postal_code / _pdbx_contact_author.state_province / _pdbx_poly_seq_scheme.auth_mon_id / _pdbx_poly_seq_scheme.auth_seq_num / _pdbx_poly_seq_scheme.pdb_mon_id / _refine.B_iso_mean / _refine.aniso_B[1][1] / _refine.aniso_B[1][3] / _refine.aniso_B[2][2] / _refine.aniso_B[3][3] / _refine.correlation_coeff_Fo_to_Fc / _refine.details / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_all / _refine.ls_R_factor_obs / _refine.ls_d_res_high / _refine.ls_d_res_low / _refine.ls_number_reflns_R_work / _refine.ls_number_reflns_obs / _refine.ls_percent_reflns_R_free / _refine.ls_percent_reflns_obs / _refine.ls_wR_factor_R_free / _refine.ls_wR_factor_R_work / _refine.overall_SU_B / _refine.overall_SU_ML / _refine.pdbx_average_fsc_free / _refine.pdbx_average_fsc_work / _refine.pdbx_overall_ESU_R_Free / _refine.solvent_model_details / _refine_hist.cycle_id / _refine_hist.d_res_high / _refine_hist.d_res_low / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_protein / _reflns.d_resolution_high / _reflns.d_resolution_low / _software.version
Description: Real space R-factor / Provider: author / Type: Coordinate replacement

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Histone H3.1
B: Histone H4
C: Histone H2A type 1-B/E
D: Histone H2B type 1-J
E: Histone H3.1
F: Histone H4
G: Histone H2A type 1-B/E
H: Histone H2B type 1-J
I: DNA (169-MER)
J: DNA (169-MER)
K: Histone H3.1
L: Histone H4
M: Histone H2A type 1-B/E
N: Histone H2B type 1-J
O: Histone H3.1
P: Histone H4
Q: Histone H2A type 1-B/E
R: Histone H2B type 1-J
S: DNA (169-MER)
T: DNA (169-MER)
U: Histone H3.1
V: Histone H4
W: Histone H2A type 1-B/E
X: Histone H2B type 1-J
Y: Histone H3.1
Z: Histone H4
a: Histone H2A type 1-B/E
b: Histone H2B type 1-J
c: DNA (169-MER)
d: DNA (169-MER)
e: Histone H3.1
f: Histone H4
g: Histone H2A type 1-B/E
h: Histone H2B type 1-J
i: Histone H3.1
j: Histone H4
k: Histone H2A type 1-B/E
l: Histone H2B type 1-J
m: DNA (169-MER)
n: DNA (169-MER)
o: Histone H1.0


Theoretical massNumber of molelcules
Total (without water)882,37541
Polymers882,37541
Non-polymers00
Water0
1
A: Histone H3.1
B: Histone H4
C: Histone H2A type 1-B/E
D: Histone H2B type 1-J
E: Histone H3.1
F: Histone H4
G: Histone H2A type 1-B/E
H: Histone H2B type 1-J
I: DNA (169-MER)
J: DNA (169-MER)
U: Histone H3.1
V: Histone H4
W: Histone H2A type 1-B/E
X: Histone H2B type 1-J
Y: Histone H3.1
Z: Histone H4
a: Histone H2A type 1-B/E
b: Histone H2B type 1-J
c: DNA (169-MER)
d: DNA (169-MER)
o: Histone H1.0


Theoretical massNumber of molelcules
Total (without water)451,66321
Polymers451,66321
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
K: Histone H3.1
L: Histone H4
M: Histone H2A type 1-B/E
N: Histone H2B type 1-J
O: Histone H3.1
P: Histone H4
Q: Histone H2A type 1-B/E
R: Histone H2B type 1-J
S: DNA (169-MER)
T: DNA (169-MER)
e: Histone H3.1
f: Histone H4
g: Histone H2A type 1-B/E
h: Histone H2B type 1-J
i: Histone H3.1
j: Histone H4
k: Histone H2A type 1-B/E
l: Histone H2B type 1-J
m: DNA (169-MER)
n: DNA (169-MER)


Theoretical massNumber of molelcules
Total (without water)430,71320
Polymers430,71320
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)213.850, 102.460, 218.289
Angle α, β, γ (deg.)90.000, 100.490, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 5 types, 33 molecules AEKOUYeiBFLPVZfjCGMQWagkDHNRXb...

#1: Protein
Histone H3.1 / Histone H3 / Histone H3/a / Histone H3/b / Histone H3/c / Histone H3/d / Histone H3/f / Histone H3/h / Histone ...Histone H3/a / Histone H3/b / Histone H3/c / Histone H3/d / Histone H3/f / Histone H3/h / Histone H3/i / Histone H3/j / Histone H3/k / Histone H3/l


Mass: 15581.299 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: H3C1, H3FA, HIST1H3A, H3C2, H3FL, HIST1H3B, H3C3, H3FC HIST1H3C, H3C4, H3FB, HIST1H3D, H3C6, H3FD, HIST1H3E, H3C7, H3FI, HIST1H3F, H3C8, H3FH, HIST1H3G, H3C10, H3FK, HIST1H3H, H3C11, H3FF, ...Gene: H3C1, H3FA, HIST1H3A, H3C2, H3FL, HIST1H3B, H3C3, H3FC HIST1H3C, H3C4, H3FB, HIST1H3D, H3C6, H3FD, HIST1H3E, H3C7, H3FI, HIST1H3F, H3C8, H3FH, HIST1H3G, H3C10, H3FK, HIST1H3H, H3C11, H3FF, HIST1H3I, H3C12, H3FJ, HIST1H3J
Production host: Escherichia coli (E. coli) / References: UniProt: P68431
#2: Protein
Histone H4 /


Mass: 11538.556 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: H4C1, H4/A, H4FA, HIST1H4A, H4C2, H4/I, H4FI, HIST1H4B, H4C3, H4/G, H4FG, HIST1H4C, H4C4, H4/B, H4FB, HIST1H4D, H4C5, H4/J, H4FJ, HIST1H4E, H4C6, H4/C, H4FC, HIST1H4F, H4C8, H4/H, H4FH, ...Gene: H4C1, H4/A, H4FA, HIST1H4A, H4C2, H4/I, H4FI, HIST1H4B, H4C3, H4/G, H4FG, HIST1H4C, H4C4, H4/B, H4FB, HIST1H4D, H4C5, H4/J, H4FJ, HIST1H4E, H4C6, H4/C, H4FC, HIST1H4F, H4C8, H4/H, H4FH, HIST1H4H, H4C9, H4/M, H4FM, HIST1H4I, H4C11, H4/E, H4FE, HIST1H4J, H4C12, H4/D, H4FD, HIST1H4K, H4C13, H4/K, H4FK, HIST1H4L, H4C14, H4/N, H4F2, H4FN, HIST2H4, HIST2H4A, H4C15, H4/O, H4FO, HIST2H4B, H4-16, HIST4H4
Production host: Escherichia coli (E. coli) / References: UniProt: P62805
#3: Protein
Histone H2A type 1-B/E / Histone H2A.2 / Histone H2A/a / Histone H2A/m


Mass: 14309.679 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: H2AC4, H2AFM, HIST1H2AB, H2AC8, H2AFA, HIST1H2AE / Production host: Escherichia coli (E. coli) / References: UniProt: P04908
#4: Protein
Histone H2B type 1-J / Histone H2B.1 / Histone H2B.r / H2B/r


Mass: 14079.370 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: H2BC11, H2BFR, HIST1H2BJ / Production host: Escherichia coli (E. coli) / References: UniProt: P06899
#7: Protein Histone H1.0 / Histone H1' / Histone H1(0)


Mass: 20950.152 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: H1-0, H1F0, H1FV / Production host: Escherichia coli (E. coli) / References: UniProt: P07305

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DNA chain , 2 types, 8 molecules IScmJTdn

#5: DNA chain
DNA (169-MER)


Mass: 52008.266 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli (E. coli)
#6: DNA chain
DNA (169-MER)


Mass: 52330.262 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli (E. coli)

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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: 2.66 Å3/Da / Density % sol: 53.85 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / Details: 40-45mM CaCl2, 25mM KCl, 10mM Na-acetate (pH 4.5)

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Data collection

DiffractionMean temperature: 98.15 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Sep 17, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.506→88.439 Å / Num. obs: 117231 / % possible obs: 100 % / Redundancy: 6.1 % / CC1/2: 1 / Net I/σ(I): 8
Reflection shellResolution: 3.51→3.57 Å / Redundancy: 5.9 % / Mean I/σ(I) obs: 1.1 / Num. unique obs: 5763 / CC1/2: 0.37 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0258refinement
iMOSFLMdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3UT9, 4QLC

3ut9

4qlc


Resolution: 3.506→88.439 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.928 / WRfactor Rfree: 0.273 / WRfactor Rwork: 0.2 / SU B: 43.628 / SU ML: 0.639 / Average fsc free: 0.8426 / Average fsc work: 0.8744 / Cross valid method: THROUGHOUT / ESU R Free: 0.691
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflectionSelection details
Rfree0.2795 2266 2.015 %RANDOM
Rwork0.2062 110177 --
all0.208 ---
obs-112443 95.918 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 147.315 Å2
Baniso -1Baniso -2Baniso -3
1-0.062 Å2-0 Å20.533 Å2
2---2.352 Å2-0 Å2
3---1.958 Å2
Refinement stepCycle: LAST / Resolution: 3.506→88.439 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24850 27724 0 0 52574
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.01256274
X-RAY DIFFRACTIONr_bond_other_d0.0020.01840511
X-RAY DIFFRACTIONr_angle_refined_deg1.3491.37881804
X-RAY DIFFRACTIONr_angle_other_deg1.4362.12794249
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.98553097
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.57118.5681459
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.075154829
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.32515351
X-RAY DIFFRACTIONr_chiral_restr0.0730.27374
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0244201
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0212588
X-RAY DIFFRACTIONr_nbd_refined0.2010.212941
X-RAY DIFFRACTIONr_symmetry_nbd_other0.2160.244994
X-RAY DIFFRACTIONr_nbtor_refined0.2110.223563
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0790.220495
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.160.21332
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.0710.268
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.3340.277
X-RAY DIFFRACTIONr_nbd_other0.4370.2143
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.3850.210
X-RAY DIFFRACTIONr_mcbond_it9.49711.99412487
X-RAY DIFFRACTIONr_mcbond_other9.49211.99412486
X-RAY DIFFRACTIONr_mcangle_it14.43217.94115551
X-RAY DIFFRACTIONr_mcangle_other14.43317.94215552
X-RAY DIFFRACTIONr_scbond_it12.14317.28643787
X-RAY DIFFRACTIONr_scbond_other12.14217.28643785
X-RAY DIFFRACTIONr_scangle_it19.23725.9466253
X-RAY DIFFRACTIONr_scangle_other19.23725.9466253
X-RAY DIFFRACTIONr_lrange_it24.996171.02474372
X-RAY DIFFRACTIONr_lrange_other24.996171.02574373
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.506-3.5970.4651610.3897544X-RAY DIFFRACTION89.5202
3.597-3.6960.3881600.3467467X-RAY DIFFRACTION90.3673
3.696-3.8030.3791450.3267309X-RAY DIFFRACTION91.8772
3.803-3.920.3561420.2847250X-RAY DIFFRACTION93.2156
3.92-4.0480.341440.2387155X-RAY DIFFRACTION94.6938
4.048-4.190.321460.2366926X-RAY DIFFRACTION95.041
4.19-4.3480.2861440.2016807X-RAY DIFFRACTION96.8645
4.348-4.5260.2781250.1866571X-RAY DIFFRACTION96.889
4.526-4.7270.2451230.1926359X-RAY DIFFRACTION97.6058
4.727-4.9580.2851310.1886110X-RAY DIFFRACTION98.0827
4.958-5.2260.2511190.1645830X-RAY DIFFRACTION98.3306
5.226-5.5420.271270.1725538X-RAY DIFFRACTION98.7106
5.542-5.9250.3561080.2065249X-RAY DIFFRACTION98.7647
5.925-6.3990.3421100.2184853X-RAY DIFFRACTION98.7662
6.399-7.0090.296940.1984483X-RAY DIFFRACTION99.1981
7.009-7.8350.264820.1644136X-RAY DIFFRACTION99.7399
7.835-9.0460.188610.1523657X-RAY DIFFRACTION99.8389
9.046-11.0740.194610.1523112X-RAY DIFFRACTION99.9055
11.074-15.640.201540.1632423X-RAY DIFFRACTION99.9596
15.64-88.4390.218290.2291398X-RAY DIFFRACTION99.1661

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