[English] 日本語
Yorodumi
- PDB-3oj4: Crystal structure of the A20 ZnF4, ubiquitin and UbcH5A complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3oj4
TitleCrystal structure of the A20 ZnF4, ubiquitin and UbcH5A complex
Components
  • Tumor necrosis factor alpha-induced protein 3
  • Ubiquitin-conjugating enzyme E2 D1
  • Ubiquitin
KeywordsLIGASE/PROTEIN BINDING / ubiquitin / zinc finger / ubiquitin conjugating enzyme / zinc ion / LIGASE-PROTEIN BINDING complex
Function / homology
Function and homology information


regulation of vascular wound healing / negative regulation of toll-like receptor 5 signaling pathway / negative regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway / establishment of protein localization to vacuole / negative regulation of osteoclast proliferation / tolerance induction to lipopolysaccharide / negative regulation of CD40 signaling pathway / negative regulation of toll-like receptor 3 signaling pathway / negative regulation of B cell activation / negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway ...regulation of vascular wound healing / negative regulation of toll-like receptor 5 signaling pathway / negative regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway / establishment of protein localization to vacuole / negative regulation of osteoclast proliferation / tolerance induction to lipopolysaccharide / negative regulation of CD40 signaling pathway / negative regulation of toll-like receptor 3 signaling pathway / negative regulation of B cell activation / negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / negative regulation of toll-like receptor 2 signaling pathway / protein K11-linked deubiquitination / positive regulation of protein polyubiquitination / negative regulation of chronic inflammatory response / : / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / negative regulation of toll-like receptor 4 signaling pathway / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / Aberrant regulation of mitotic exit in cancer due to RB1 defects / regulation of germinal center formation / (E3-independent) E2 ubiquitin-conjugating enzyme / B-1 B cell homeostasis / protein K48-linked deubiquitination / Phosphorylation of the APC/C / Signaling by BMP / regulation of defense response to virus by host / regulation of tumor necrosis factor-mediated signaling pathway / Transferases; Acyltransferases; Aminoacyltransferases / protein K63-linked deubiquitination / positive regulation of hepatocyte proliferation / hypothalamus gonadotrophin-releasing hormone neuron development / negative regulation of bone resorption / female meiosis I / positive regulation of protein monoubiquitination / TNFR1-induced proapoptotic signaling / mitochondrion transport along microtubule / K63-linked polyubiquitin modification-dependent protein binding / E2 ubiquitin-conjugating enzyme / fat pad development / negative regulation of interleukin-2 production / negative regulation of interleukin-1 beta production / K63-linked deubiquitinase activity / female gonad development / negative regulation of NF-kappaB transcription factor activity / seminiferous tubule development / male meiosis I / protein deubiquitination / ubiquitin conjugating enzyme activity / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / negative regulation of interleukin-6 production / Regulation of APC/C activators between G1/S and early anaphase / response to muramyl dipeptide / positive regulation of Wnt signaling pathway / negative regulation of tumor necrosis factor production / negative regulation of BMP signaling pathway / Transcriptional Regulation by VENTX / protein K48-linked ubiquitination / regulation of proteasomal protein catabolic process / ubiquitin ligase complex / negative regulation of endothelial cell apoptotic process / energy homeostasis / regulation of neuron apoptotic process / negative regulation of canonical NF-kappaB signal transduction / cytoskeleton organization / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / negative regulation of protein ubiquitination / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / negative regulation of TORC1 signaling / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Constitutive Signaling by NOTCH1 HD Domain Mutants / Endosomal Sorting Complex Required For Transport (ESCRT) / NOTCH2 Activation and Transmission of Signal to the Nucleus / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3 / Regulation of FZD by ubiquitination / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / APC-Cdc20 mediated degradation of Nek2A / PINK1-PRKN Mediated Mitophagy / TRAF6-mediated induction of TAK1 complex within TLR4 complex / InlA-mediated entry of Listeria monocytogenes into host cells / Pexophagy / Regulation of innate immune responses to cytosolic DNA / VLDLR internalisation and degradation
Similarity search - Function
Zinc finger, A20-type / A20-like zinc finger / Zinc finger A20-type profile. / A20-like zinc fingers / OTU-like cysteine protease / OTU domain / OTU domain profile. / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site ...Zinc finger, A20-type / A20-like zinc finger / Zinc finger A20-type profile. / A20-like zinc fingers / OTU-like cysteine protease / OTU domain / OTU domain profile. / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme/RWD-like / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin domain signature. / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin-like domain / Ubiquitin domain profile. / Ubiquitin-like domain superfamily / Roll / Alpha Beta
Similarity search - Domain/homology
Polyubiquitin-B / Polyubiquitin-C / Tumor necrosis factor alpha-induced protein 3 / Ubiquitin-conjugating enzyme E2 D1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.4 Å
AuthorsBosanac, I. / Hymowitz, S.G.
CitationJournal: Mol.Cell / Year: 2010
Title: Ubiquitin Binding to A20 ZnF4 Is Required for Modulation of NF-κB Signaling
Authors: Bosanac, I. / Wertz, I.E. / Pan, B. / Yu, C. / Kusam, S. / Lam, C. / Phu, L. / Phung, Q. / Maurer, B. / Arnott, D. / Kirkpatrick, D.S. / Dixit, V.M. / Hymowitz, S.G.
History
DepositionAug 20, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 8, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Jan 24, 2018Group: Structure summary / Category: audit_author / Item: _audit_author.name
Revision 1.3Sep 6, 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_conn_angle / struct_conn / struct_ncs_dom_lim / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Ubiquitin-conjugating enzyme E2 D1
B: Ubiquitin
C: Tumor necrosis factor alpha-induced protein 3
D: Ubiquitin-conjugating enzyme E2 D1
E: Ubiquitin
F: Tumor necrosis factor alpha-induced protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,2418
Polymers63,1106
Non-polymers1312
Water0
1
A: Ubiquitin-conjugating enzyme E2 D1
B: Ubiquitin
C: Tumor necrosis factor alpha-induced protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,6204
Polymers31,5553
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Ubiquitin-conjugating enzyme E2 D1
E: Ubiquitin
F: Tumor necrosis factor alpha-induced protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,6204
Polymers31,5553
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)102.646, 102.646, 112.686
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number150
Space group name H-MP321
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21D
12B
22E
13C
23F

NCS domain segments:

Component-ID: 1 / Refine code: 2

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11METMETMETMETAA1 - 1477 - 153
21METMETMETMETDD1 - 1477 - 153
12METMETARGARGBB1 - 724 - 75
22METMETARGARGEE1 - 724 - 75
13SERSERLYSLYSCC605 - 63519 - 49
23SERSERLYSLYSFF605 - 63519 - 49

NCS ensembles :
ID
1
2
3

-
Components

#1: Protein Ubiquitin-conjugating enzyme E2 D1 / Ubiquitin-protein ligase D1 / Ubiquitin carrier protein D1 / UbcH5 / Ubiquitin-conjugating enzyme ...Ubiquitin-protein ligase D1 / Ubiquitin carrier protein D1 / UbcH5 / Ubiquitin-conjugating enzyme E2-17 kDa 1 / Ubiquitin-conjugating enzyme E2(17)KB 1 / UBC4/5 homolog / Stimulator of Fe transport / SFT


Mass: 17277.756 Da / Num. of mol.: 2 / Fragment: Ubiquitin-conjugating enzyme E2 D1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2D1, SFT, UBC5A, UBCH5, UBCH5A / Plasmid: pET-15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) codon + RIL / References: UniProt: P51668, ubiquitin-protein ligase
#2: Protein Ubiquitin /


Mass: 8859.106 Da / Num. of mol.: 2 / Fragment: Ubiquitin, UNP residues 1-76
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Plasmid: pET-15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) codon + RIL / References: UniProt: P0CG47, UniProt: P0CG48*PLUS
#3: Protein/peptide Tumor necrosis factor alpha-induced protein 3 / TNF alpha-induced protein 3 / OTU domain-containing protein 7C / Putative DNA-binding protein A20 / ...TNF alpha-induced protein 3 / OTU domain-containing protein 7C / Putative DNA-binding protein A20 / Zinc finger protein A20


Mass: 5418.088 Da / Num. of mol.: 2 / Fragment: Zinc finger A20-type 4, UNP residues 592-635
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TNFAIP3, OTUD7C / Plasmid: pET-15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) codon + RIL / References: UniProt: P21580
#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.72 Å3/Da / Density % sol: 54.7 %
Crystal growTemperature: 292 K / Method: vapor diffusion / pH: 7.1
Details: 0.1 M HEPES pH 7.1 and 1.85 M Na Malonate pH 7.0, VAPOR DIFFUSION, temperature 292K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Oct 13, 2006
RadiationMonochromator: Asymmetric curved crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.4→25 Å / Num. all: 9814 / Num. obs: 9637 / % possible obs: 98.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 6.1 % / Rsym value: 0.115 / Net I/σ(I): 16.8
Reflection shellResolution: 3.4→3.52 Å / Redundancy: 3.9 % / Mean I/σ(I) obs: 3.3 / Num. unique all: 955 / Rsym value: 0.75 / % possible all: 99.8

-
Processing

Software
NameVersionClassification
BOSdata collection
PHASERphasing
REFMAC5.2.0019refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY: 1UBQ, 1X23

1ubq

1x23


Resolution: 3.4→25 Å / Cor.coef. Fo:Fc: 0.876 / Cor.coef. Fo:Fc free: 0.842 / SU B: 102.112 / SU ML: 0.724 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.767 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.31882 962 10 %RANDOM
Rwork0.27984 ---
all0.284 9612 --
obs0.28381 8650 98.09 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 94.095 Å2
Baniso -1Baniso -2Baniso -3
1--3.19 Å2-1.6 Å20 Å2
2---3.19 Å20 Å2
3---4.79 Å2
Refinement stepCycle: LAST / Resolution: 3.4→25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3986 0 2 0 3988
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0224090
X-RAY DIFFRACTIONr_angle_refined_deg1.0131.9755538
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.3135494
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.84824.556180
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.90915722
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.3951520
X-RAY DIFFRACTIONr_chiral_restr0.070.2608
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.023074
X-RAY DIFFRACTIONr_nbd_refined0.1940.21669
X-RAY DIFFRACTIONr_nbtor_refined0.3020.22715
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1250.2127
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.3230.2127
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2080.25
X-RAY DIFFRACTIONr_mcbond_it0.8342.52587
X-RAY DIFFRACTIONr_mcangle_it1.28154086
X-RAY DIFFRACTIONr_scbond_it1.2532.51707
X-RAY DIFFRACTIONr_scangle_it1.82351452
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A588tight positional0.010.05
2B288tight positional0.020.05
3C124tight positional0.010.05
1A582medium positional0.150.5
2B286medium positional0.180.5
3C125medium positional0.090.5
1A588tight thermal0.020.5
2B288tight thermal0.020.5
3C124tight thermal0.020.5
1A582medium thermal0.162
2B286medium thermal0.152
3C125medium thermal0.142
LS refinement shellResolution: 3.4→3.469 Å / Rfactor Rfree error: 43.6 / Total num. of bins used: 25
RfactorNum. reflection% reflection
Rfree0.436 61 -
Rwork0.43 502 -
obs-563 100 %
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)
113.26093.45892.42286.15513.63810.1513-0.2905-0.43070.3014-0.41240.3140.4103-1.03571.1709-0.0234-0.5801-0.0904-0.0359-0.48410.0597-0.4289-36.746120.302664.2197
26.33641.94091.777415.37054.606510.6419-0.78081.04660.3943-2.19311.3058-0.2936-2.32311.9386-0.5250.5577-0.90760.03980.1725-0.141-0.4883-25.919517.78943.6012
350.84428.46463.222342.261114.996344.9484-0.36651.3702-4.13350.11521.5811-1.95161.82132.8831-1.2146-0.7426-0.0592-0.1028-0.2453-0.2041-0.2868-27.7701-4.393844.3441
45.417-1.70571.184414.22524.487210.34870.60.03230.23120.0111-0.64260.49081.6588-0.25490.0426-0.38850.01550.0786-0.6307-0.0109-0.4151-35.94721.6829-7.8757
510.83254.62864.00299.832.473110.34151.1882-0.843-0.56922.1166-0.46780.20282.3933-0.7979-0.72041.0243-0.5801-0.1239-0.2837-0.037-0.4339-28.349313.53512.7369
638.92950.04227.175852.13968.345538.17170.64730.16770.47371.64470.5544-4.14331.2432.7195-1.2016-0.28060.2274-0.0646-0.6408-0.1888-0.318-10.087126.250212.0151
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 147
2X-RAY DIFFRACTION2B1 - 73
3X-RAY DIFFRACTION3C605 - 635
4X-RAY DIFFRACTION4D1 - 147
5X-RAY DIFFRACTION5E1 - 73
6X-RAY DIFFRACTION6F605 - 635

+
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