[English] 日本語
Yorodumi
- PDB-7t2d: Crystal structure of the B1 TCR in complex with HLA-DP4-Ply -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7t2d
TitleCrystal structure of the B1 TCR in complex with HLA-DP4-Ply
Components
  • (HLA class II histocompatibility antigen, DP ...) x 2
  • (T cell receptor, B1, ...) x 2
  • Pneumolysin-derived peptide
KeywordsIMMUNE SYSTEM / TCR-pHLA complex
Function / homology
Function and homology information


MHC class II receptor activity / alpha-beta T cell receptor complex / cholesterol binding / transport vesicle membrane / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / alpha-beta T cell activation / Generation of second messenger molecules / PD-1 signaling / positive regulation of T cell proliferation ...MHC class II receptor activity / alpha-beta T cell receptor complex / cholesterol binding / transport vesicle membrane / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / alpha-beta T cell activation / Generation of second messenger molecules / PD-1 signaling / positive regulation of T cell proliferation / MHC class II antigen presentation / trans-Golgi network membrane / lumenal side of endoplasmic reticulum membrane / response to bacterium / clathrin-coated endocytic vesicle membrane / ER to Golgi transport vesicle membrane / cellular response to type II interferon / peptide antigen assembly with MHC class II protein complex / MHC class II protein complex / positive regulation of type II interferon production / peptide antigen binding / antigen processing and presentation of exogenous peptide antigen via MHC class II / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / positive regulation of immune response / Interferon gamma signaling / endocytic vesicle membrane / positive regulation of T cell activation / Downstream TCR signaling / MHC class II protein complex binding / late endosome membrane / T cell receptor signaling pathway / toxin activity / killing of cells of another organism / adaptive immune response / immune response / lysosomal membrane / Golgi membrane / intracellular membrane-bounded organelle / host cell plasma membrane / cell surface / extracellular region / membrane / plasma membrane
Similarity search - Function
Thiol-activated cytolysins signature. / Thiol-activated cytolysin C-terminal / Thiol-activated cytolysin, C-terminal domain superfamily / Thiol-activated cytolysin beta sandwich domain / Thiol-activated cytolysin / Thiol-activated cytolysin superfamily / Thiol-activated cytolysin, alpha-beta domain superfamily / Thiol-activated cytolysin / : / T-cell receptor alpha chain, constant domain ...Thiol-activated cytolysins signature. / Thiol-activated cytolysin C-terminal / Thiol-activated cytolysin, C-terminal domain superfamily / Thiol-activated cytolysin beta sandwich domain / Thiol-activated cytolysin / Thiol-activated cytolysin superfamily / Thiol-activated cytolysin, alpha-beta domain superfamily / Thiol-activated cytolysin / : / T-cell receptor alpha chain, constant domain / Domain of unknown function (DUF1968) / MHC class II, beta chain, N-terminal / Class II histocompatibility antigen, beta domain / Class II histocompatibility antigen, beta domain / MHC class II, alpha chain, N-terminal / Class II histocompatibility antigen, alpha domain / Class II histocompatibility antigen, alpha domain / MHC class II, alpha/beta chain, N-terminal / : / MHC classes I/II-like antigen recognition protein / : / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
T cell receptor alpha chain constant / T cell receptor beta constant 1 / HLA class II histocompatibility antigen, DP beta 1 chain / HLA class II histocompatibility antigen, DP alpha 1 chain / Pneumolysin
Similarity search - Component
Biological speciesHomo sapiens (human)
Streptococcus pneumoniae (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.4 Å
AuthorsCiacchi, L. / Farenc, C. / Petersen, J. / Reid, H.H. / Rossjohn, J.
Funding support Australia, 1items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia) Australia
CitationJournal: Immunity / Year: 2023
Title: CD4 + T cell-mediated recognition of a conserved cholesterol-dependent cytolysin epitope generates broad antibacterial immunity.
Authors: Ciacchi, L. / van de Garde, M.D.B. / Ladell, K. / Farenc, C. / Poelen, M.C.M. / Miners, K.L. / Llerena, C. / Reid, H.H. / Petersen, J. / Price, D.A. / Rossjohn, J. / van Els, C.A.C.M.
History
DepositionDec 3, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 28, 2022Provider: repository / Type: Initial release
Revision 1.1Jul 12, 2023Group: Data collection / Database references / Category: citation / citation_author / diffrn_source
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _diffrn_source.pdbx_synchrotron_site
Revision 1.2Oct 25, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / diffrn_source / pdbx_initial_refinement_model
Item: _diffrn_source.pdbx_synchrotron_site

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: HLA class II histocompatibility antigen, DP alpha 1 chain
B: HLA class II histocompatibility antigen, DP beta 1 chain
C: Pneumolysin-derived peptide
F: HLA class II histocompatibility antigen, DP alpha 1 chain
G: HLA class II histocompatibility antigen, DP beta 1 chain
H: Pneumolysin-derived peptide
D: T cell receptor, B1, alpha chain
E: T cell receptor, B1, beta chain
I: T cell receptor, B1, alpha chain
J: T cell receptor, B1, beta chain
K: HLA class II histocompatibility antigen, DP alpha 1 chain
L: HLA class II histocompatibility antigen, DP beta 1 chain
M: Pneumolysin-derived peptide
N: T cell receptor, B1, alpha chain
O: T cell receptor, B1, beta chain
P: HLA class II histocompatibility antigen, DP alpha 1 chain
Q: HLA class II histocompatibility antigen, DP beta 1 chain
R: Pneumolysin-derived peptide
S: T cell receptor, B1, alpha chain
T: T cell receptor, B1, beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)385,01032
Polymers380,57020
Non-polymers4,44012
Water1267
1
A: HLA class II histocompatibility antigen, DP alpha 1 chain
B: HLA class II histocompatibility antigen, DP beta 1 chain
C: Pneumolysin-derived peptide
D: T cell receptor, B1, alpha chain
E: T cell receptor, B1, beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,3348
Polymers95,1435
Non-polymers1,1913
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
F: HLA class II histocompatibility antigen, DP alpha 1 chain
G: HLA class II histocompatibility antigen, DP beta 1 chain
H: Pneumolysin-derived peptide
I: T cell receptor, B1, alpha chain
J: T cell receptor, B1, beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,3348
Polymers95,1435
Non-polymers1,1913
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
K: HLA class II histocompatibility antigen, DP alpha 1 chain
L: HLA class II histocompatibility antigen, DP beta 1 chain
M: Pneumolysin-derived peptide
N: T cell receptor, B1, alpha chain
O: T cell receptor, B1, beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,1728
Polymers95,1435
Non-polymers1,0293
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
P: HLA class II histocompatibility antigen, DP alpha 1 chain
Q: HLA class II histocompatibility antigen, DP beta 1 chain
R: Pneumolysin-derived peptide
S: T cell receptor, B1, alpha chain
T: T cell receptor, B1, beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,1728
Polymers95,1435
Non-polymers1,0293
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)159.709, 193.570, 236.799
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212

-
Components

-
HLA class II histocompatibility antigen, DP ... , 2 types, 8 molecules AFKPBGLQ

#1: Protein
HLA class II histocompatibility antigen, DP alpha 1 chain / DP(W3) / DP(W4) / HLA-SB alpha chain / MHC class II DP3-alpha / MHC class II DPA1


Mass: 20943.336 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-DPA1, HLA-DP1A, HLASB / Cell line (production host): High Five / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P20036
#2: Protein
HLA class II histocompatibility antigen, DP beta 1 chain / HLA class II histocompatibility antigen / DP(W4) beta chain / MHC class II antigen DPB1


Mass: 21916.570 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-DPB1, HLA-DP1B / Cell line (production host): High Five / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P04440

-
T cell receptor, B1, ... , 2 types, 8 molecules DINSEJOT

#4: Protein
T cell receptor, B1, alpha chain


Mass: 23295.541 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TRAC, TCRA / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P01848
#5: Protein
T cell receptor, B1, beta chain


Mass: 27161.129 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TRBC1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P01850

-
Protein/peptide / Non-polymers , 2 types, 11 molecules CHMR

#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Formula: H2O
#3: Protein/peptide
Pneumolysin-derived peptide


Mass: 1825.995 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus pneumoniae (bacteria) / Gene: ply, SPD_1726 / Cell line (production host): High Five / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q04IN8

-
Sugars , 4 types, 12 molecules

#6: 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: isolated from a genetically manipulated source
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
#7: 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.: 1
Source method: isolated from a genetically manipulated source
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
#8: 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.: 2
Source method: isolated from a genetically manipulated source
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
#9: 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.: 8
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 ligand of interestN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 4.58 Å3/Da / Density % sol: 73.13 %
Crystal growTemperature: 277.15 K / Method: vapor diffusion, hanging drop / Details: Potassium sodium tartrate, Tris-HCl pH 8

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.95373 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 12, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.95373 Å / Relative weight: 1
ReflectionResolution: 3.4→33.4 Å / Num. obs: 101100 / % possible obs: 99.5 % / Redundancy: 2 % / CC1/2: 0.995 / Net I/σ(I): 5.6
Reflection shellResolution: 3.4→3.5 Å / Redundancy: 2 % / Mean I/σ(I) obs: 1.5 / Num. unique obs: 9986 / CC1/2: 0.691

-
Processing

Software
NameVersionClassification
PHENIX1.18.2_3874refinement
PDB_EXTRACT3.27data extraction
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4P5K, 4MAY
Resolution: 3.4→33.4 Å / SU ML: 0.47 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 32.23 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2712 5020 4.98 %
Rwork0.2364 95794 -
obs0.2382 100814 99.58 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 248.98 Å2 / Biso mean: 103.2742 Å2 / Biso min: 30 Å2
Refinement stepCycle: final / Resolution: 3.4→33.4 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms25951 0 290 7 26248
Biso mean--152.41 57.57 -
Num. residues----3218
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00327077
X-RAY DIFFRACTIONf_angle_d0.50236856
X-RAY DIFFRACTIONf_dihedral_angle_d18.6399799
X-RAY DIFFRACTIONf_chiral_restr0.0434009
X-RAY DIFFRACTIONf_plane_restr0.0034826
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
3.4-3.440.40451590.35913162100
3.44-3.480.4151340.35383180100
3.48-3.520.36081800.34713156100
3.52-3.570.37091610.32963159100
3.57-3.610.3391650.31563146100
3.61-3.660.34171580.30963192100
3.66-3.710.36051810.30243178100
3.71-3.770.36191750.29893149100
3.77-3.830.31291550.28993169100
3.83-3.890.37381710.26983184100
3.89-3.960.28191740.26113136100
3.96-4.030.27251810.24913186100
4.03-4.110.27911610.24573187100
4.11-4.190.26471580.23773172100
4.19-4.280.25941780.2287314599
4.28-4.380.24461560.21963201100
4.38-4.490.221820.20323182100
4.49-4.610.26111570.20033191100
4.61-4.750.21251550.1939319199
4.75-4.90.22391550.20023193100
4.9-5.070.23361380.20443216100
5.07-5.280.23941680.21123216100
5.28-5.520.26511860.21823188100
5.52-5.810.25522000.21953184100
5.81-6.170.29811700.23263233100
6.17-6.640.26551560.23123246100
6.64-7.30.27051610.21683239100
7.3-8.340.2072010.19893239100
8.34-10.460.18911780.18363300100
10.46-33.40.30841660.243327495
Refinement TLS params.Method: refined / Origin x: -39.9831 Å / Origin y: -17.5639 Å / Origin z: -59.2047 Å
111213212223313233
T0.7539 Å20.0456 Å2-0.0101 Å2-0.698 Å2-0.0672 Å2--0.7926 Å2
L0.0212 °20.0039 °20.0681 °2--0.0748 °2-0.0622 °2--0.1247 °2
S0.0185 Å °-0.0171 Å °0.0448 Å °-0.0034 Å °-0.0339 Å °0.0002 Å °-0.0015 Å °-0.0111 Å °0.007 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1allA1 - 180
2X-RAY DIFFRACTION1allA181 - 185
3X-RAY DIFFRACTION1allB2 - 188
4X-RAY DIFFRACTION1allC-2 - 11
5X-RAY DIFFRACTION1allF1 - 180
6X-RAY DIFFRACTION1allF181 - 185
7X-RAY DIFFRACTION1allG2 - 187
8X-RAY DIFFRACTION1allG188
9X-RAY DIFFRACTION1allH-2 - 11
10X-RAY DIFFRACTION1allD1 - 216
11X-RAY DIFFRACTION1allE9 - 257
12X-RAY DIFFRACTION1allI1 - 216
13X-RAY DIFFRACTION1allJ7 - 257
14X-RAY DIFFRACTION1allK1 - 180
15X-RAY DIFFRACTION1allK181 - 184
16X-RAY DIFFRACTION1allL2 - 190
17X-RAY DIFFRACTION1allM-2 - 11
18X-RAY DIFFRACTION1allN1 - 214
19X-RAY DIFFRACTION1allO6 - 257
20X-RAY DIFFRACTION1allP1 - 180
21X-RAY DIFFRACTION1allP181 - 184
22X-RAY DIFFRACTION1allQ2 - 188
23X-RAY DIFFRACTION1allQ189
24X-RAY DIFFRACTION1allR-2 - 11
25X-RAY DIFFRACTION1allS1 - 214
26X-RAY DIFFRACTION1allT6 - 257
27X-RAY DIFFRACTION1allU1 - 7

+
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