[English] 日本語
Yorodumi
- PDB-5kdm: Crystal structure of EBV tegument protein BNRF1 in complex with h... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5kdm
TitleCrystal structure of EBV tegument protein BNRF1 in complex with histone chaperone DAXX and histones H3.3-H4
Components
  • Death domain-associated protein 6
  • Histone H3.3
  • Histone H4
  • Major tegument protein
KeywordsCHAPERONE / DNA BINDING PROTEIN / histone chaperone / Gene repression / CHAPERONE - DNA BINDING PROTEIN complex
Function / homology
Function and homology information


cellular response to diamide / Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations / Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations / intracellular transport of virus / neuron intrinsic apoptotic signaling pathway in response to oxidative stress / cellular response to sodium arsenite / viral tegument / negative regulation of chromosome condensation / Barr body / regulation of centromere complex assembly ...cellular response to diamide / Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations / Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations / intracellular transport of virus / neuron intrinsic apoptotic signaling pathway in response to oxidative stress / cellular response to sodium arsenite / viral tegument / negative regulation of chromosome condensation / Barr body / regulation of centromere complex assembly / pericentric heterochromatin formation / inner kinetochore / muscle cell differentiation / transcription regulator inhibitor activity / oocyte maturation / nuclear androgen receptor binding / nucleus organization / protein kinase activator activity / androgen receptor signaling pathway / regulation of protein ubiquitination / chromosome, centromeric region / spermatid development / extrinsic apoptotic signaling pathway via death domain receptors / cellular response to unfolded protein / subtelomeric heterochromatin formation / single fertilization / positive regulation of protein kinase activity / negative regulation of megakaryocyte differentiation / RNA polymerase II core promoter sequence-specific DNA binding / protein localization to CENP-A containing chromatin / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / JNK cascade / heat shock protein binding / Deposition of new CENPA-containing nucleosomes at the centromere / cellular response to copper ion / nucleosomal DNA binding / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / cellular response to cadmium ion / telomere organization / embryo implantation / Meiotic synapsis / RNA Polymerase I Promoter Opening / Assembly of the ORC complex at the origin of replication / SUMOylation of chromatin organization proteins / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / DNA methylation / SUMOylation of transcription cofactors / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Chromatin modifications during the maternal to zygotic transition (MZT) / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / HCMV Late Events / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / HDACs deacetylate histones / Nonhomologous End-Joining (NHEJ) / RNA Polymerase I Promoter Escape / molecular condensate scaffold activity / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / NoRC negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / G2/M DNA damage checkpoint / HDMs demethylate histones / B-WICH complex positively regulates rRNA expression / multicellular organism growth / DNA Damage/Telomere Stress Induced Senescence / PML body / PKMTs methylate histone lysines / Meiotic recombination / Pre-NOTCH Transcription and Translation / RMTs methylate histone arginines / Activation of anterior HOX genes in hindbrain development during early embryogenesis / HCMV Early Events / Transcriptional regulation of granulopoiesis / osteoblast differentiation / male gonad development / structural constituent of chromatin / transcription corepressor activity / nucleosome / host cell / p53 binding / Regulation of TP53 Degradation / nucleosome assembly / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / chromatin organization / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / HATs acetylate histones / cellular response to heat / Processing of DNA double-strand break ends
Similarity search - Function
Herpes virus tegument protein / Tegument protein, herpes virus, N-terminal domain / dsDNA viral tegument protein / Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #2170 / Daxx, N-terminal Rassf1C-interacting domain / Daxx, N-terminal domain superfamily / Daxx, histone-binding domain / Daxx, histone-binding domain superfamily / Daxx N-terminal Rassf1C-interacting domain / Death domain-associated protein 6, histone binding domain ...Herpes virus tegument protein / Tegument protein, herpes virus, N-terminal domain / dsDNA viral tegument protein / Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #2170 / Daxx, N-terminal Rassf1C-interacting domain / Daxx, N-terminal domain superfamily / Daxx, histone-binding domain / Daxx, histone-binding domain superfamily / Daxx N-terminal Rassf1C-interacting domain / Death domain-associated protein 6, histone binding domain / CobB/CobQ-like glutamine amidotransferase domain / CobB/CobQ-like glutamine amidotransferase domain / PurM-like, C-terminal domain / PurM-like, C-terminal domain superfamily / PurM-like, N-terminal domain superfamily / AIR synthase related protein, C-terminal domain / Histone, subunit A / Histone, subunit A / Class I glutamine amidotransferase-like / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / 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 / Up-down Bundle / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Histone H4 / Histone H3.3 / Major tegument protein / Death domain-associated protein 6
Similarity search - Component
Biological speciesHomo sapiens (human)
Epstein-Barr virus (Epstein-Barr virus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 Å
AuthorsHuang, H. / Patel, D.
CitationJournal: Nat Commun / Year: 2016
Title: Structural basis underlying viral hijacking of a histone chaperone complex.
Authors: Huang, H. / Deng, Z. / Vladimirova, O. / Wiedmer, A. / Lu, F. / Lieberman, P.M. / Patel, D.J.
History
DepositionJun 8, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 7, 2016Provider: repository / Type: Initial release
Revision 1.1May 16, 2018Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Source and taxonomy
Category: citation / citation_author ...citation / citation_author / entity_src_gen / pdbx_struct_oper_list
Item: _citation.page_first / _citation.page_last ..._citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name / _entity_src_gen.pdbx_host_org_scientific_name / _pdbx_struct_oper_list.symmetry_operation
Revision 1.2Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Experimental preparation / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / exptl_crystal / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _exptl_crystal.density_Matthews / _exptl_crystal.density_percent_sol

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Histone H3.3
B: Histone H4
C: Death domain-associated protein 6
D: Major tegument protein


Theoretical massNumber of molelcules
Total (without water)74,6334
Polymers74,6334
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)161.216, 161.216, 117.772
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221

-
Components

#1: Protein Histone H3.3


Mass: 15229.787 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: H3F3A, H3.3A, H3F3, PP781, H3F3B, H3.3B / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3)-codon plus / References: UniProt: P84243
#2: Protein Histone H4


Mass: 11263.231 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, ...Gene: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4
Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3)-codon plus / References: UniProt: P62805
#3: Protein Death domain-associated protein 6 / Daxx / hDaxx / ETS1-associated protein 1 / EAP1 / Fas death domain-associated protein


Mass: 24725.328 Da / Num. of mol.: 1 / Fragment: residues 178-389
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: DAXX, BING2, DAP6 / Production host: Escherichia coli BL21(DE3) coli (bacteria) / Strain (production host): BL21(DE3)-codon plus / References: UniProt: Q9UER7
#4: Protein Major tegument protein / MTP / Protein p140


Mass: 23414.498 Da / Num. of mol.: 1 / Fragment: residues 381-599
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Epstein-Barr virus (strain AG876) / Strain: AG876 / Gene: BNRF1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3)-codon plus / References: UniProt: Q1HVJ0

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 5.92 Å3/Da / Density % sol: 79.22 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 6 / Details: 0.1M MES pH 6.0, 0.8 M ammonium sulfate

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.979 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Dec 10, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 3.4→50 Å / Num. obs: 22487 / % possible obs: 99.2 % / Redundancy: 11 % / Net I/σ(I): 14.6
Reflection shellResolution: 3.4→3.73 Å / Redundancy: 10.7 % / Mean I/σ(I) obs: 0.9 / % possible all: 99.1

-
Processing

Software
NameVersionClassification
PHENIXdev_1839refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4H9N

4h9n


Resolution: 3.5→48.157 Å / SU ML: 0.65 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 34.22
RfactorNum. reflection% reflection
Rfree0.2796 1134 5.04 %
Rwork0.2345 --
obs0.2368 22487 99.16 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 3.5→48.157 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4341 0 0 0 4341
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0134418
X-RAY DIFFRACTIONf_angle_d1.6835975
X-RAY DIFFRACTIONf_dihedral_angle_d18.7031656
X-RAY DIFFRACTIONf_chiral_restr0.062674
X-RAY DIFFRACTIONf_plane_restr0.01783
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.4974-3.65650.3841440.37572615X-RAY DIFFRACTION98
3.6565-3.84920.38171390.3452625X-RAY DIFFRACTION99
3.8492-4.09030.30861250.30662645X-RAY DIFFRACTION99
4.0903-4.40590.29571400.26522643X-RAY DIFFRACTION99
4.4059-4.84890.30691450.22762653X-RAY DIFFRACTION99
4.8489-5.54970.2521540.22152676X-RAY DIFFRACTION99
5.5497-6.98860.27951350.26562706X-RAY DIFFRACTION99
6.9886-48.16160.24581520.1762790X-RAY DIFFRACTION99
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)
10.68770.8384-0.76990.7997-0.42150.24780.27340.24310.71031.5177-0.583-0.381.21550.9257-0.00471.1479-0.21680.13551.46570.03631.5116-0.8411-73.8828-8.4967
20.47840.1864-0.773-0.0001-0.54830.63830.8531.74650.2880.2748-0.3586-1.8257-0.38971.18530.00221.31650.04940.15351.7676-0.01441.24428.097-70.7517-21.7987
31.01650.08940.39631.64892.13752.0526-0.3132.025-0.3575-0.4994-0.37750.4908-0.38491.968-0.00551.41150.20190.18932.135-0.17451.241520.1207-74.1355-39.6488
41.9599-0.63841.70560.1972-0.34730.9280.54370.15410.237-0.8553-1.07890.4091-0.05120.0866-0.00251.13110.00710.06511.40950.11091.362617.8889-61.4049-26.924
50.8115-0.3626-0.37320.15810.27080.353.8426-0.03160.34861.4115-3.86761.1561-2.76860.1402-0.00351.8338-0.13050.34781.61190.10041.611715.0526-40.1377-28.0438
60.5486-0.016-0.13390.0879-0.28720.03880.07020.57310.47380.2467-0.20590.5996-1.60770.78370.00150.9627-0.0148-0.04061.3333-0.11991.476626.1064-48.497-27.8847
70.78870.74790.1022.1634-1.24861.0751-0.50480.56231.69510.602-0.97042.081.2695-3.227-0.00251.17360.1358-0.22771.3008-0.03631.6159.0496-56.6256-34.8126
81.9498-0.1138-1.61940.1571-0.21082.09691.09753.6180.75830.12960.1036-1.03620.0798-4.609-0.0161.59210.397-0.0671.85590.09641.829510.7726-47.4165-31.0117
9-0.02390.42970.99230.95890.81584.78770.4290.4486-0.1136-1.5502-0.1533-0.30.24890.04430.00030.9885-0.18670.05151.56940.24081.696125.1551-65.2312-34.9155
100.1107-0.20030.180.1407-0.2590.34771.49163.62030.7077-0.7812-1.136-1.21.79060.0621-0.01411.21960.27560.10711.3747-0.18481.857128.4111-84.0033-31.3692
111.98880.5965-0.89880.266-0.66651.45660.012-0.2203-1.0360.82890.1848-0.9308-0.18241.194201.15270.22150.12851.6757-0.09671.204626.7876-69.9949-21.094
120.9436-0.71310.70733.045-1.30231.15360.7612-0.5781-1.65210.8751-0.8339-1.3306-0.6170.9714-0.01261.31970.0198-0.22481.38380.1021.2854-0.6262-84.6413-19.1378
130.88472.13861.56741.15461.01374.2326-0.2053-0.06950.3027-0.24730.10890.7348-0.14360.0026-0.00061.39970.13510.10841.4309-0.05631.27515.0282-68.5307-21.0955
143.49-1.6550.29291.245-1.0571.61610.3996-0.63171.0094-1.0729-1.01390.3363-2.2343-2.51630.00421.93620.27720.37261.4587-0.11942.08495.5559-43.5241-14.4514
151.2457-0.19410.20672.9678-2.08190.6746-0.11790.01230.7445-0.0265-0.1614-0.4017-0.1480.3020.00071.35440.0367-0.07771.4066-0.0031.413124.0149-57.6821-21.9661
163.87650.00870.20473.1547-3.50063.0810.12950.1074-0.73940.26220.45140.1815-0.1729-0.33020.00331.2192-0.1083-0.01511.0126-0.0581.316718.0622-82.33460.8554
172.47763.0822-1.13174.9025-2.27251.90240.1399-0.6748-0.23241.2599-0.6243-1.21770.38350.297-0.00011.34050.0024-0.24941.34880.01431.282119.9511-80.01017.6435
181.75290.4985-1.21540.28280.03540.7588-0.2139-1.29230.36341.76740.308-0.7783-0.13530.54090.00521.517-0.0637-0.30281.5907-0.07441.29624.0415-69.71928.28
194.44820.1099-3.42972.5131-1.34143.1523-0.3356-0.2841-0.05740.2635-0.04450.480.1619-0.5967-0.00091.1969-0.07920.01491.33080.03341.41968.7416-83.77565.6928
201.5508-0.1461.38742.423-1.76371.53041.3127-0.93550.0150.8828-1.2678-0.2313-1.1960.00330.01171.45130.11430.011.3546-0.2581.293913.7714-66.95350.5588
210.49450.1322-0.54841.2594-1.37950.54750.18771.57751.52540.9144-0.91180.058-0.96060.3730.00381.2875-0.2481-0.11041.8731-0.0921.602319.0787-67.7711-2.801
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 37 through 47 )
2X-RAY DIFFRACTION2chain 'A' and (resid 48 through 63 )
3X-RAY DIFFRACTION3chain 'A' and (resid 64 through 85 )
4X-RAY DIFFRACTION4chain 'A' and (resid 86 through 109 )
5X-RAY DIFFRACTION5chain 'A' and (resid 110 through 120 )
6X-RAY DIFFRACTION6chain 'A' and (resid 121 through 135 )
7X-RAY DIFFRACTION7chain 'B' and (resid 26 through 40 )
8X-RAY DIFFRACTION8chain 'B' and (resid 41 through 47 )
9X-RAY DIFFRACTION9chain 'B' and (resid 48 through 75 )
10X-RAY DIFFRACTION10chain 'B' and (resid 76 through 82 )
11X-RAY DIFFRACTION11chain 'B' and (resid 83 through 102 )
12X-RAY DIFFRACTION12chain 'C' and (resid 182 through 207 )
13X-RAY DIFFRACTION13chain 'C' and (resid 208 through 266 )
14X-RAY DIFFRACTION14chain 'C' and (resid 267 through 299 )
15X-RAY DIFFRACTION15chain 'C' and (resid 300 through 386 )
16X-RAY DIFFRACTION16chain 'D' and (resid 383 through 413 )
17X-RAY DIFFRACTION17chain 'D' and (resid 414 through 488 )
18X-RAY DIFFRACTION18chain 'D' and (resid 489 through 512 )
19X-RAY DIFFRACTION19chain 'D' and (resid 513 through 546 )
20X-RAY DIFFRACTION20chain 'D' and (resid 547 through 564 )
21X-RAY DIFFRACTION21chain 'D' and (resid 565 through 581 )

+
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