[English] 日本語
Yorodumi
- PDB-8suf: The complex of TOL-1 ectodomain bound to LAT-1 Lectin domain -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8suf
TitleThe complex of TOL-1 ectodomain bound to LAT-1 Lectin domain
Components
  • Latrophilin-like protein 1
  • TIR domain-containing protein
KeywordsCELL ADHESION / Cell Surface Receptor
Function / homology
Function and homology information


Class B/2 (Secretin family receptors) / : / Signaling by EGFR / Negative regulation of MET activity / Neutrophil degranulation / sexual reproduction / self proteolysis / embryo development ending in birth or egg hatching / anterior/posterior pattern specification / extracellular matrix ...Class B/2 (Secretin family receptors) / : / Signaling by EGFR / Negative regulation of MET activity / Neutrophil degranulation / sexual reproduction / self proteolysis / embryo development ending in birth or egg hatching / anterior/posterior pattern specification / extracellular matrix / G protein-coupled receptor activity / adenylate cyclase-activating G protein-coupled receptor signaling pathway / defense response / transmembrane signaling receptor activity / carbohydrate binding / defense response to Gram-negative bacterium / endopeptidase activity / cell surface receptor signaling pathway / extracellular space / membrane / plasma membrane
Similarity search - Function
: / D-galactoside/L-rhamnose binding SUEL lectin domain superfamily / GAIN domain, N-terminal / GPCR-Autoproteolysis INducing (GAIN) domain / D-galactoside/L-rhamnose binding SUEL lectin domain / Galactose binding lectin domain / SUEL-type lectin domain profile. / GAIN domain superfamily / GPCR proteolysis site, GPS, motif / GPS motif ...: / D-galactoside/L-rhamnose binding SUEL lectin domain superfamily / GAIN domain, N-terminal / GPCR-Autoproteolysis INducing (GAIN) domain / D-galactoside/L-rhamnose binding SUEL lectin domain / Galactose binding lectin domain / SUEL-type lectin domain profile. / GAIN domain superfamily / GPCR proteolysis site, GPS, motif / GPS motif / GAIN-B domain profile. / G-protein-coupled receptor proteolytic site domain / TIR domain / Leucine-rich repeats, bacterial type / Toll - interleukin 1 - resistance / Hormone receptor domain / GPCR, family 2, extracellular hormone receptor domain / G-protein coupled receptors family 2 profile 1. / Domain present in hormone receptors / GPCR family 2, extracellular hormone receptor domain superfamily / TIR domain profile. / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily / GPCR, family 2, secretin-like / 7 transmembrane receptor (Secretin family) / GPCR, family 2-like / G-protein coupled receptors family 2 profile 2. / 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
Similarity search - Domain/homology
Latrophilin-like protein 1 / TIR domain-containing protein
Similarity search - Component
Biological speciesCaenorhabditis elegans (invertebrata)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4 Å
AuthorsCarmona Rosas, G. / Li, J. / Arac, D. / Ozkan, E.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35 GM148412 United States
CitationJournal: To Be Published
Title: Structural basis and functional roles for Toll-like receptor binding to Latrophilin adhesion-GPCR in embryo development
Authors: Carmona Rosas, G. / Li, J. / Smith, J.S. / Cheng, S. / Baltrusaitis, E. / Nawrocka, W.I. / Zhao, M. / Kratsios, P. / Arac, D. / Ozkan, E.
History
DepositionMay 12, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 15, 2024Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: TIR domain-containing protein
B: TIR domain-containing protein
C: TIR domain-containing protein
D: TIR domain-containing protein
E: Latrophilin-like protein 1
F: Latrophilin-like protein 1
G: Latrophilin-like protein 1
H: Latrophilin-like protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)507,33728
Polymers499,2608
Non-polymers8,07720
Water00
1
A: TIR domain-containing protein
E: Latrophilin-like protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)127,0768
Polymers124,8152
Non-polymers2,2616
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: TIR domain-containing protein
F: Latrophilin-like protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)127,4008
Polymers124,8152
Non-polymers2,5856
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: TIR domain-containing protein
G: Latrophilin-like protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)126,5936
Polymers124,8152
Non-polymers1,7784
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: TIR domain-containing protein
H: Latrophilin-like protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)126,2686
Polymers124,8152
Non-polymers1,4534
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)74.152, 316.755, 172.441
Angle α, β, γ (deg.)90.000, 90.160, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1(chain "A" and (resid 27 through 695 or resid 700 through 983 or resid 2011 through 2021))
d_2ens_1(chain "B" and (resid 27 through 983 or resid 2011 through 2012))
d_3ens_1(chain "C" and (resid 27 through 695 or resid 700 through 983 or resid 2011 through 2051))
d_4ens_1(chain "D" and (resid 27 through 695 or resid 700 through 983 or resid 2011 through 2012))
d_1ens_2(chain "E" and resid 29 through 133)
d_2ens_2(chain "F" and resid 29 through 133)
d_3ens_2(chain "G" and resid 29 through 133)
d_4ens_2chain "H"

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_11ens_1GLUGLUASPASPAA27 - 69534 - 702
d_12ens_1TYRTYRPROPROAA700 - 983707 - 990
d_13ens_1NAGNAGNAGNAGAS1101
d_14ens_1NAGNAGNAGNAGII1
d_21ens_1GLUGLUPROPROBB27 - 98334 - 990
d_22ens_1NAGNAGNAGNAGLL1
d_23ens_1NAGNAGNAGNAGLL2
d_31ens_1GLUGLUASPASPCC27 - 69534 - 702
d_32ens_1TYRTYRPROPROCC700 - 983707 - 990
d_33ens_1NAGNAGNAGNAGCY1101
d_34ens_1NAGNAGNAGNAGOO1
d_41ens_1GLUGLUASPASPDD27 - 69534 - 702
d_42ens_1TYRTYRPROPRODD700 - 983707 - 990
d_43ens_1NAGNAGNAGNAGQQ1
d_44ens_1NAGNAGNAGNAGQQ2
d_11ens_2ALAALACYSCYSEE29 - 1331 - 105
d_21ens_2ALAALACYSCYSFF29 - 1331 - 105
d_31ens_2ALAALACYSCYSGG29 - 1331 - 105
d_41ens_2ALAALACYSCYSHH29 - 1331 - 105

NCS ensembles :
ID
ens_1
ens_2

NCS oper:
IDCodeMatrixVector
1given(0.991581021888, -0.108698702074, -0.070368097874), (0.0937964797422, 0.977602974934, -0.188400222365), (0.0892709214637, 0.18021380515, 0.979568112494)6.76331798568, -25.8179928654, 77.0929598037
2given(0.997217536701, 0.0502163798141, -0.0550953690801), (0.048660395391, -0.998387600554, -0.0292295223955), (-0.056474334136, 0.0264672298786, -0.998053172595)-42.7732900247, -70.3529746457, -215.32723102
3given(0.98953847067, -0.14029034673, -0.0336486801966), (-0.132337624748, -0.975541394619, 0.175515641639), (-0.0574488306282, -0.169226493193, -0.983901430968)-26.3521670021, -40.6888892904, -121.720994022
4given(0.999496217222, 0.006520727343, 0.0310610990508), (-0.00771317070308, 0.999231662362, 0.0384264483304), (-0.030786665247, -0.0386466693067, 0.998778562142)12.0117911248, 4.8140900998, 93.8123259241
5given(0.98897947898, -0.0454680643682, -0.140897996011), (-0.0554116305268, -0.996181316225, -0.0674710041899), (-0.137292175158, 0.0745348262669, -0.987722338673)-49.1824492667, -69.3506008928, -211.440484054
6given(0.553821096507, -0.80559741031, 0.210463786827), (-0.789753355633, -0.588312795886, -0.173717274511), (0.263764725333, -0.0700061904339, -0.962043295788)73.2716480206, -48.5753259301, -141.102728397

-
Components

-
Protein , 2 types, 8 molecules ABCDEFGH

#1: Protein
TIR domain-containing protein


Mass: 112253.797 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: Construct is secreted by a signal peptide, cleaved and not present in mature protein, and has N-terminal His and Avi tags.
Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: tol-1, C07F11.1, CELE_C07F11.1 / Cell line (production host): High Five cells / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q9N5Z3
#2: Protein
Latrophilin-like protein 1


Mass: 12561.144 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: Construct is secreted by a signal peptide, cleaved and not present in mature protein, and has a C-terminal His-tag. Contains isoform a for LAT-1 protein.
Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: lat-1, B0457.1 / Variant: isoform a / Cell line (production host): High Five cells / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: G5EDW2

-
Sugars , 6 types, 20 molecules

#3: Polysaccharide alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 2 / Source method: obtained synthetically
DescriptorTypeProgram
DManpa1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c6-d1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#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.: 5
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam 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
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#5: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1 / Source method: obtained synthetically
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#6: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1 / Source method: obtained synthetically
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#7: 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.: 1 / Source method: obtained synthetically
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam 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
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}LINUCSPDB-CARE
#8: 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.: 10 / Source method: obtained synthetically / 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 ligand of interestN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 4.37 Å3/Da / Density % sol: 71.86 %
Crystal growTemperature: 297 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 0.2 M Sodium Malonate, 0.1 M Bis-Tris Propane pH 7.5, 26% PEG 3350, 1.2% Myo-Inositol

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97918 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 30, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 4→200 Å / Num. obs: 37159 / % possible obs: 55.6 % / Redundancy: 3.4 % / Biso Wilson estimate: 139.85 Å2 / CC1/2: 0.996 / Rmerge(I) obs: 0.112 / Rsym value: 0.112 / Net I/σ(I): 6.2
Reflection shellResolution: 4→4.42 Å / Rmerge(I) obs: 0.727 / Mean I/σ(I) obs: 2.1 / Num. unique obs: 2858 / CC1/2: 0.603 / Rsym value: 0.727 / % possible all: 16.7

-
Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
XDSdata reduction
STARANISOdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 4→74.15 Å / SU ML: 0.8107 / Cross valid method: FREE R-VALUE / Phase error: 48.2417
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.3377 1858 5.01 %
Rwork0.2883 35233 -
obs0.2908 37091 55.54 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 197.65 Å2
Refinement stepCycle: LAST / Resolution: 4→74.15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms32463 0 530 0 32993
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.006533537
X-RAY DIFFRACTIONf_angle_d1.080745503
X-RAY DIFFRACTIONf_chiral_restr0.05855516
X-RAY DIFFRACTIONf_plane_restr0.00695830
X-RAY DIFFRACTIONf_dihedral_angle_d11.475212683
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2AAX-RAY DIFFRACTIONTorsion NCS7.09361746616
ens_1d_3AAX-RAY DIFFRACTIONTorsion NCS1.64289511289
ens_1d_4AAX-RAY DIFFRACTIONTorsion NCS7.80906715893
ens_2d_2EEX-RAY DIFFRACTIONTorsion NCS0.44868721748
ens_2d_3EEX-RAY DIFFRACTIONTorsion NCS0.772750042714
ens_2d_4EEX-RAY DIFFRACTIONTorsion NCS0.727044050531
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
4-4.110.4627240.3205477X-RAY DIFFRACTION9.69
4.11-4.230.403470.3333759X-RAY DIFFRACTION16.04
4.23-4.370.3695690.31091032X-RAY DIFFRACTION21.14
4.37-4.520.276650.28541437X-RAY DIFFRACTION29.85
4.52-4.710.35421090.271794X-RAY DIFFRACTION36.79
4.71-4.920.28821110.25372185X-RAY DIFFRACTION44.74
4.92-5.180.32991380.26572624X-RAY DIFFRACTION54.24
5.18-5.50.30011910.27883044X-RAY DIFFRACTION63.01
5.5-5.930.32521800.29243586X-RAY DIFFRACTION73.54
5.93-6.520.38181770.30034154X-RAY DIFFRACTION84.39
6.52-7.470.36772500.32094527X-RAY DIFFRACTION92.33
7.47-9.410.38362510.33234826X-RAY DIFFRACTION98.43
9.41-74.150.31112460.26214788X-RAY DIFFRACTION97.09

+
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://pdbjlvh1.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