[English] 日本語
Yorodumi
- PDB-3a79: Crystal structure of TLR2-TLR6-Pam2CSK4 complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3a79
TitleCrystal structure of TLR2-TLR6-Pam2CSK4 complex
Components
  • (Toll-like receptor ...) x 2
  • Pam2CSK4
KeywordsIMMUNE SYSTEM / Toll-like Receptor / diacyl lipopeptide / innate immunity / Leucine Rich Repeat / Cell membrane / Cytoplasmic vesicle / Disulfide bond / Glycoprotein / Immune response / Inflammatory response / LEUCINE-RICH REPEAT / Membrane / Receptor / Transmembrane / Phosphoprotein
Function / homology
Function and homology information


diacyl lipopeptide binding / Beta defensins / triacyl lipopeptide binding / Toll-like receptor 2-Toll-like receptor 6 protein complex / detection of diacyl bacterial lipopeptide / cellular response to diacyl bacterial lipopeptide / positive regulation of neutrophil migration / Toll-like receptor 1-Toll-like receptor 2 protein complex / detection of triacyl bacterial lipopeptide / cellular response to triacyl bacterial lipopeptide ...diacyl lipopeptide binding / Beta defensins / triacyl lipopeptide binding / Toll-like receptor 2-Toll-like receptor 6 protein complex / detection of diacyl bacterial lipopeptide / cellular response to diacyl bacterial lipopeptide / positive regulation of neutrophil migration / Toll-like receptor 1-Toll-like receptor 2 protein complex / detection of triacyl bacterial lipopeptide / cellular response to triacyl bacterial lipopeptide / cellular response to bacterial lipopeptide / lipoteichoic acid binding / negative regulation of synapse assembly / Regulation of TLR by endogenous ligand / response to molecule of fungal origin / lipopeptide binding / regulation of dendritic cell cytokine production / response to peptidoglycan / positive regulation of interleukin-18 production / cellular response to oxidised low-density lipoprotein particle stimulus / positive regulation of xenophagy / xenophagy / neutrophil migration / negative regulation of actin filament polymerization / cell surface pattern recognition receptor signaling pathway / TRIF-dependent toll-like receptor signaling pathway / cellular response to peptidoglycan / negative regulation of interleukin-12 production / positive regulation of macrophage activation / NAD+ nucleosidase activity, cyclic ADP-ribose generating / microglia development / negative regulation of interleukin-17 production / positive regulation of cytokine production involved in inflammatory response / positive regulation of synapse assembly / positive regulation of extrinsic apoptotic signaling pathway / positive regulation of leukocyte migration / positive regulation of intracellular signal transduction / MyD88-dependent toll-like receptor signaling pathway / positive regulation of macrophage cytokine production / negative regulation of phagocytosis / leukocyte migration / positive regulation of reactive oxygen species biosynthetic process / positive regulation of NLRP3 inflammasome complex assembly / pattern recognition receptor activity / : / cellular response to lipoteichoic acid / negative regulation of tumor necrosis factor production / positive regulation of chemokine production / nitric oxide biosynthetic process / Neutrophil degranulation / positive regulation of interleukin-12 production / ERK1 and ERK2 cascade / axonogenesis / positive regulation of interferon-beta production / positive regulation of interleukin-1 beta production / learning / positive regulation of cytokine production / response to bacterium / defense response / positive regulation of interleukin-6 production / positive regulation of inflammatory response / phagocytic vesicle membrane / positive regulation of tumor necrosis factor production / transmembrane signaling receptor activity / positive regulation of nitric oxide biosynthetic process / amyloid-beta binding / positive regulation of canonical NF-kappaB signal transduction / positive regulation of ERK1 and ERK2 cascade / defense response to Gram-positive bacterium / inflammatory response / membrane raft / external side of plasma membrane / innate immune response / positive regulation of gene expression / protein-containing complex binding / Golgi apparatus / positive regulation of transcription by RNA polymerase II / identical protein binding / membrane / plasma membrane
Similarity search - Function
Variable lymphocyte receptor, C-terminal / Domain of unknown function (DUF3439) / Toll-like receptor / : / Leucine rich repeat N-terminal domain / Leucine rich repeat 4 / Leucine Rich repeats (2 copies) / Leucine-rich repeat N-terminal domain / Leucine rich repeat N-terminal domain / TIR domain ...Variable lymphocyte receptor, C-terminal / Domain of unknown function (DUF3439) / Toll-like receptor / : / Leucine rich repeat N-terminal domain / Leucine rich repeat 4 / Leucine Rich repeats (2 copies) / Leucine-rich repeat N-terminal domain / Leucine rich repeat N-terminal domain / TIR domain / Leucine Rich repeat / Cysteine-rich flanking region, C-terminal / Leucine rich repeat C-terminal domain / Toll - interleukin 1 - resistance / Leucine-rich repeats, bacterial type / Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) / Ribonuclease Inhibitor / TIR domain profile. / Alpha-Beta Horseshoe / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily / Leucine rich repeat / Leucine-rich repeat, typical subtype / Leucine-rich repeats, typical (most populated) subfamily / Leucine-rich repeat profile. / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Alpha Beta
Similarity search - Domain/homology
(2S)-propane-1,2-diyl dihexadecanoate / Variable lymphocyte receptor B / Variable lymphocyte receptor B / Toll-like receptor 6 / Toll-like receptor 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
Eptatretus burgeri (inshore hagfish)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsKang, J.Y. / Jin, M.S. / Lee, J.-O.
CitationJournal: Immunity / Year: 2009
Title: Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer
Authors: Kang, J.Y. / Nan, X. / Jin, M.S. / Youn, S.-J. / Ryu, Y.H. / Mah, S. / Han, S.H. / Lee, H. / Paik, S.-G. / Lee, J.-O.
History
DepositionSep 20, 2009Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 24, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.2Jun 27, 2012Group: Non-polymer description
Revision 1.3Aug 9, 2017Group: Source and taxonomy / Category: entity_src_gen
Revision 1.4Aug 16, 2017Group: Source and taxonomy / Category: pdbx_entity_src_syn
Item: _pdbx_entity_src_syn.ncbi_taxonomy_id / _pdbx_entity_src_syn.organism_scientific
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / database_PDB_caveat / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_chiral / struct_asym / struct_conn / struct_ref_seq / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq.db_align_beg / _struct_ref_seq.db_align_end / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Nov 1, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Toll-like receptor 2, Variable lymphocyte receptor B
B: Toll-like receptor 6, Variable lymphocyte receptor B
C: Pam2CSK4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,73815
Polymers130,0463
Non-polymers4,69212
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7620 Å2
ΔGint53 kcal/mol
Surface area47840 Å2
MethodPISA
Unit cell
Length a, b, c (Å)168.901, 168.901, 231.353
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122

-
Components

-
Toll-like receptor ... , 2 types, 2 molecules AB

#1: Protein Toll-like receptor 2, Variable lymphocyte receptor B / TLR2 / VLRB.61


Mass: 65535.309 Da / Num. of mol.: 1
Fragment: extracellular domain, UNP residues 1-506(mouse), UNP residues 133-200(Inshore hagfish)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse), (gene. exp.) Eptatretus burgeri (inshore hagfish)
Gene: Tlr2 / Plasmid: PVL1393 / Production host: TRICHOPLUSIA NI (cabbage looper) / Strain (production host): Hi-5 / References: UniProt: Q9QUN7, UniProt: Q4G1L2
#2: Protein Toll-like receptor 6, Variable lymphocyte receptor B / TLR6 / VLRB.59


Mass: 63785.551 Da / Num. of mol.: 1
Fragment: extracellular domain, UNP residues 1-482(mouse), UNP residues 157-232(Inshore hagfish)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse), (gene. exp.) Eptatretus burgeri (inshore hagfish)
Gene: Tlr6 / Plasmid: PVL1393 / Production host: TRICHOPLUSIA NI (cabbage looper) / Strain (production host): Hi-5 / References: UniProt: Q9EPW9, UniProt: Q4G1L3

-
Protein/peptide / Non-polymers , 2 types, 2 molecules C

#3: Protein/peptide Pam2CSK4


Mass: 724.955 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic peptide / Source: (synth.) synthetic construct (others)
#7: Chemical ChemComp-PXS / (2S)-propane-1,2-diyl dihexadecanoate


Mass: 552.912 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C35H68O4

-
Sugars , 3 types, 11 molecules

#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#5: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#6: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

-
Details

Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.66 Å3/Da / Density % sol: 66.39 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: 2.0M ammonium sulfate, 0.1M MES pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8726 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Sep 24, 2008
RadiationMonochromator: Silicon 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8726 Å / Relative weight: 1
ReflectionResolution: 2.9→50 Å / Num. all: 43746 / Num. obs: 43573 / % possible obs: 99.67 % / Observed criterion σ(I): -3 / Redundancy: 3.4 % / Biso Wilson estimate: 56.99 Å2 / Rsym value: 0.106 / Net I/σ(I): 8.27
Reflection shellResolution: 2.9→3 Å / Redundancy: 3.55 % / Mean I/σ(I) obs: 2.33 / Num. unique all: 3448 / Rsym value: 0.525 / % possible all: 98.4

-
Processing

Software
NameVersionClassificationNB
PHENIXrefinement
PDB_EXTRACT3.005data extraction
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 2Z81, 2Z7X, 2O6R

2z81

2z7x

2o6r


Resolution: 2.9→34.11 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.799 / SU ML: 2.75 / σ(F): 0 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.28 4429 10.16 %
Rwork0.208 --
obs0.215 43573 99.67 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 31.282 Å2 / ksol: 0.278 e/Å3
Displacement parametersBiso max: 445.89 Å2 / Biso mean: 88.661 Å2 / Biso min: 24.01 Å2
Baniso -1Baniso -2Baniso -3
1--1.214 Å20 Å2-0 Å2
2---1.214 Å20 Å2
3----28.384 Å2
Refinement stepCycle: LAST / Resolution: 2.9→34.11 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8596 0 310 0 8906
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0089122
X-RAY DIFFRACTIONf_angle_d1.25112385
X-RAY DIFFRACTIONf_chiral_restr0.0761479
X-RAY DIFFRACTIONf_plane_restr0.0041526
X-RAY DIFFRACTIONf_dihedral_angle_d22.8583482
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection allNum. reflection obs% reflection obs (%)
2.9-2.9330.4121320.34128014121280100
2.933-2.9670.3981510.301128514361285100
2.967-3.0040.3541440.304128114251281100
3.004-3.0420.3771420.284127814201278100
3.042-3.0820.3331590.27128014391280100
3.082-3.1240.3161540.249127714311277100
3.124-3.1680.3371490.246125914081259100
3.168-3.2160.3311460.243129014361290100
3.216-3.2660.3171420.229129414361294100
3.266-3.3190.3191440.228128014241280100
3.319-3.3770.3191450.22130114461301100
3.377-3.4380.2851500.211128814381288100
3.438-3.5040.2981220.198130614281306100
3.504-3.5750.2841460.196130614521306100
3.575-3.6530.2521430.185129014331290100
3.653-3.7380.2541380.166130414421304100
3.738-3.8310.2381590.172128114401281100
3.831-3.9350.2341470.169130014471300100
3.935-4.050.2481620.17127914411279100
4.05-4.1810.2221450.16512961441129699
4.181-4.330.2481450.152131014551310100
4.33-4.5030.1981430.14512991442129999
4.503-4.7070.211470.143132014671320100
4.707-4.9550.2061550.135130414591304100
4.955-5.2640.2411430.161133814811338100
5.264-5.6690.2481490.171132714761327100
5.669-6.2360.2971590.198133614951336100
6.236-7.1320.2531440.204135615001356100
7.132-8.9580.3061670.214136515321365100
8.958-34.1110.2761570.24514341591143497
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)
12.2887-0.84010.98570.7151-0.12511.34470.20790.09340.0862-0.1321-0.0438-0.06040.27340.0322-0.14290.33030.0646-0.15180.1446-0.04880.372814.6701-35.826915.2995
21.8496-0.3520.10941.12340.02071.3299-0.0058-0.24480.1595-0.0351-0.05320.0233-0.27790.26880.05090.3214-0.0689-0.07210.3344-0.07610.279855.8446-34.550635.5039
30.6819-0.0475-0.64330.7414-0.0021-0.32020.0239-0.44670.1462-0.08660.09060.2312-0.01860.0657-0.01240.69760.0681-0.42550.6385-0.11030.619521.0865-41.919342.8576
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain AA26 - 575
2X-RAY DIFFRACTION2chain BB33 - 557
3X-RAY DIFFRACTION3chain CA - C10 - 16

+
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