[English] 日本語
Yorodumi
- PDB-7a2a: Crystal Structure of EGFR-T790M/V948R in Complex with Spebrutinib... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7a2a
TitleCrystal Structure of EGFR-T790M/V948R in Complex with Spebrutinib and EAI001
ComponentsEpidermal growth factor receptor
KeywordsTRANSFERASE / EGFR
Function / homology
Function and homology information


multivesicular body, internal vesicle lumen / negative regulation of cardiocyte differentiation / Shc-EGFR complex / positive regulation of protein kinase C signaling / Inhibition of Signaling by Overexpressed EGFR / epidermal growth factor receptor activity / EGFR interacts with phospholipase C-gamma / regulation of peptidyl-tyrosine phosphorylation / epidermal growth factor binding / response to UV-A ...multivesicular body, internal vesicle lumen / negative regulation of cardiocyte differentiation / Shc-EGFR complex / positive regulation of protein kinase C signaling / Inhibition of Signaling by Overexpressed EGFR / epidermal growth factor receptor activity / EGFR interacts with phospholipase C-gamma / regulation of peptidyl-tyrosine phosphorylation / epidermal growth factor binding / response to UV-A / PLCG1 events in ERBB2 signaling / ERBB2-EGFR signaling pathway / morphogenesis of an epithelial fold / PTK6 promotes HIF1A stabilization / ERBB2 Activates PTK6 Signaling / digestive tract morphogenesis / Signaling by EGFR / intracellular vesicle / negative regulation of epidermal growth factor receptor signaling pathway / eyelid development in camera-type eye / cerebral cortex cell migration / protein insertion into membrane / ERBB2 Regulates Cell Motility / protein tyrosine kinase activator activity / Respiratory syncytial virus (RSV) attachment and entry / Signaling by ERBB4 / PI3K events in ERBB2 signaling / positive regulation of phosphorylation / positive regulation of peptidyl-serine phosphorylation / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / hair follicle development / MAP kinase kinase kinase activity / GAB1 signalosome / positive regulation of G1/S transition of mitotic cell cycle / embryonic placenta development / salivary gland morphogenesis / Signaling by ERBB2 / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / transmembrane receptor protein tyrosine kinase activity / EGFR Transactivation by Gastrin / GRB2 events in ERBB2 signaling / ossification / SHC1 events in ERBB2 signaling / positive regulation of DNA repair / basal plasma membrane / cellular response to epidermal growth factor stimulus / positive regulation of DNA replication / epithelial cell proliferation / positive regulation of epithelial cell proliferation / Signal transduction by L1 / positive regulation of protein localization to plasma membrane / NOTCH3 Activation and Transmission of Signal to the Nucleus / cellular response to amino acid stimulus / phosphatidylinositol 3-kinase/protein kinase B signal transduction / cellular response to estradiol stimulus / EGFR downregulation / clathrin-coated endocytic vesicle membrane / Signaling by ERBB2 TMD/JMD mutants / Constitutive Signaling by EGFRvIII / cell-cell adhesion / receptor protein-tyrosine kinase / Signaling by ERBB2 ECD mutants / negative regulation of protein catabolic process / Signaling by ERBB2 KD Mutants / positive regulation of miRNA transcription / kinase binding / ruffle membrane / Downregulation of ERBB2 signaling / epidermal growth factor receptor signaling pathway / positive regulation of protein phosphorylation / cell morphogenesis / neuron differentiation / positive regulation of fibroblast proliferation / HCMV Early Events / Constitutive Signaling by Aberrant PI3K in Cancer / actin filament binding / cell junction / transmembrane signaling receptor activity / positive regulation of canonical Wnt signaling pathway / Cargo recognition for clathrin-mediated endocytosis / PIP3 activates AKT signaling / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / Clathrin-mediated endocytosis / ATPase binding / virus receptor activity / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / positive regulation of cell growth / double-stranded DNA binding / protein tyrosine kinase activity / early endosome membrane / protein phosphatase binding / nuclear membrane / basolateral plasma membrane / learning or memory / Extra-nuclear estrogen signaling / cell surface receptor signaling pathway / positive regulation of ERK1 and ERK2 cascade
Similarity search - Function
: / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain ...: / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain / Furin-like repeat / Furin-like repeats / Growth factor receptor cysteine-rich domain superfamily / : / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-57N / Chem-7G9 / Epidermal growth factor receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsNiggenaber, J. / Mueller, M.P. / Rauh, D.
Funding support Germany, 3items
OrganizationGrant numberCountry
German Federal Ministry for Education and ResearchBMBF 01GS08104 Germany
German Federal Ministry for Education and ResearchBMBF 01ZX1303C Germany
European Regional Development FundEFRE-800400 Germany
CitationJournal: Acs Med.Chem.Lett. / Year: 2020
Title: Complex Crystal Structures of EGFR with Third-Generation Kinase Inhibitors and Simultaneously Bound Allosteric Ligands.
Authors: Niggenaber, J. / Heyden, L. / Grabe, T. / Muller, M.P. / Lategahn, J. / Rauh, D.
History
DepositionAug 17, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 11, 2020Provider: repository / Type: Initial release
Revision 1.1Dec 30, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Aug 24, 2022Group: Database references / Category: database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.3Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_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
Revision 1.4Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Epidermal growth factor receptor
B: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,89711
Polymers75,9282
Non-polymers1,9699
Water2,090116
1
A: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,9666
Polymers37,9641
Non-polymers1,0025
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,9315
Polymers37,9641
Non-polymers9674
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)75.180, 83.730, 92.340
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 700 through 748 or resid 750...
21(chain B and (resid 700 through 707 or (resid 708...

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASNASNARGARG(chain A and (resid 700 through 748 or resid 750...AA700 - 74811 - 59
12ALAALAHISHIS(chain A and (resid 700 through 748 or resid 750...AA750 - 77361 - 84
13CYSCYSMETMET(chain A and (resid 700 through 748 or resid 750...AA775 - 79086 - 101
14LEULEULEULEU(chain A and (resid 700 through 748 or resid 750...AA792 - 833103 - 144
15VALVALVALVAL(chain A and (resid 700 through 748 or resid 750...AA834145
16ASNASNASPASP(chain A and (resid 700 through 748 or resid 750...AA700 - 98411 - 295
17ASNASNASPASP(chain A and (resid 700 through 748 or resid 750...AA700 - 98411 - 295
18ASNASNASPASP(chain A and (resid 700 through 748 or resid 750...AA700 - 98411 - 295
19ASNASNASPASP(chain A and (resid 700 through 748 or resid 750...AA700 - 98411 - 295
21ASNASNLEULEU(chain B and (resid 700 through 707 or (resid 708...BB700 - 70711 - 18
22LYSLYSGLUGLU(chain B and (resid 700 through 707 or (resid 708...BB708 - 70919 - 20
23PROPROASPASP(chain B and (resid 700 through 707 or (resid 708...BB699 - 98410 - 295
24PROPROASPASP(chain B and (resid 700 through 707 or (resid 708...BB699 - 98410 - 295
25PROPROASPASP(chain B and (resid 700 through 707 or (resid 708...BB699 - 98410 - 295
26PROPROASPASP(chain B and (resid 700 through 707 or (resid 708...BB699 - 98410 - 295

-
Components

-
Protein , 1 types, 2 molecules AB

#1: Protein Epidermal growth factor receptor / Proto-oncogene c-ErbB-1 / Receptor tyrosine-protein kinase erbB-1


Mass: 37963.910 Da / Num. of mol.: 2 / Mutation: T790M, V948R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EGFR, ERBB, ERBB1, HER1 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: P00533, receptor protein-tyrosine kinase

-
Non-polymers , 5 types, 125 molecules

#2: Chemical ChemComp-57N / (2R)-2-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)-2-phenyl-N-(1,3-thiazol-2-yl)acetamide


Mass: 349.406 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H15N3O2S / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-7G9 / ~{N}-[3-[[5-fluoranyl-2-[[4-(2-methoxyethoxy)phenyl]amino]pyrimidin-4-yl]amino]phenyl]propanamide


Mass: 425.456 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C22H24FN5O3 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 116 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has ligand of interestY
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 1.91 Å3/Da / Density % sol: 35.73 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 25 % PEG3350, 100 mM MgSO4, 4 % ethylen glycole, 5.0 mg/mL EGFR-T790M/V948R (in 100 mM NaCl, 25 mM Tris-HCl, 10 % glycerol, 1 mM TCEP, pH 8.0) 1 ul reservoir + 1 ul protein solution)

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9999 Å
DetectorType: DECTRIS EIGER2 X 16M / Detector: PIXEL / Date: Jun 22, 2020
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9999 Å / Relative weight: 1
ReflectionResolution: 1.9→47.84 Å / Num. obs: 46627 / % possible obs: 100 % / Redundancy: 13.27 % / CC1/2: 0.999 / Rrim(I) all: 0.063 / Net I/σ(I): 21.34
Reflection shellResolution: 1.9→2 Å / Redundancy: 14.16 % / Mean I/σ(I) obs: 2.09 / Num. unique obs: 6548 / CC1/2: 0.746 / Rrim(I) all: 1.698 / % possible all: 100

-
Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6S8A

6s8a


Resolution: 1.9→47.84 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 23.21 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2171 2331 5 %
Rwork0.1943 44286 -
obs0.1954 46617 99.98 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 126.32 Å2 / Biso mean: 57.8185 Å2 / Biso min: 29.68 Å2
Refinement stepCycle: final / Resolution: 1.9→47.84 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4112 0 133 116 4361
Biso mean--53.28 55.16 -
Num. residues----534
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A2340X-RAY DIFFRACTION9.306TORSIONAL
12B2340X-RAY DIFFRACTION9.306TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 17 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
1.9-1.940.30271350.304525802715
1.94-1.980.36011350.27825582693
1.98-2.030.29861350.256725642699
2.03-2.080.27931370.243825982735
2.08-2.130.29441340.236325422676
2.13-2.20.25111350.215525832718
2.2-2.270.25161360.216825782714
2.27-2.350.25131360.211325832719
2.35-2.440.22931360.208825842720
2.44-2.550.24041370.222125962733
2.55-2.690.23461370.212625982735
2.69-2.860.23031360.216625872723
2.86-3.080.23521370.222226142751
3.08-3.390.28071390.210926302769
3.39-3.880.21541380.182926362774
3.88-4.880.1711410.148926662807
4.88-47.840.18111470.186127892936
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)
13.4489-1.4444-0.59721.48980.52790.75870.56410.6615-0.0456-0.0645-0.0093-0.4151-0.20430.6778-0.30840.7346-0.2235-0.090.68510.05520.3656-35.6838-1.1057-7.1489
23.02851.35572.18266.356-1.894.8426-0.04861.90040.313-0.49250.3170.32080.38230.5519-0.06570.4909-0.0184-0.06640.6502-0.04360.4013-38.0651-8.2047-6.4404
32.2969-2.1584-1.46354.41850.94151.33940.34831.0029-0.3772-0.2945-0.53640.7618-0.3254-0.32640.23710.5070.0806-0.11990.5398-0.06240.3712-46.0654-1.5631-6.7182
41.66010.1776-0.09961.26970.53224.3412-0.09650.1044-0.0631-0.017-0.00490.2215-0.11110.02370.0940.32150.01090.01510.3312-0.0180.3719-40.7752-6.20929.1472
54.3981-0.5618-1.12183.05160.28172.5633-0.03240.3716-0.02030.1497-0.10270.5197-0.0902-0.39090.18690.35780.00790.06620.371-0.02740.4132-53.1875-5.70416.3848
63.02041.35640.0662.4204-0.64151.8538-0.0253-0.482-0.27650.8223-0.11560.2619-0.06440.02660.130.5605-0.02770.1530.4287-0.01230.3631-48.6019-10.900329.6528
72.3254-1.23820.64172.80341.06613.36470.0394-0.0448-0.76180.2184-0.23720.12090.34270.2110.17970.56840.00540.13870.4138-0.0620.5818-21.7349-21.21147.9689
82.3429-1.4664-1.32064.48640.24982.2087-0.1263-0.3327-0.65560.75860.1593-0.19940.49850.09380.29140.62550.07680.10.43450.03020.5162-21.1435-21.873913.7119
94.2651-0.3612-1.01834.2131-0.17422.0622-0.14670.08670.223-0.05820.2182-0.04690.14080.0882-0.09060.31680.0221-0.01210.3557-0.03480.2514-21.0087-4.61757.9312
101.83351.0244-1.13721.50660.9983.5907-0.1259-0.656-0.17950.22080.3099-0.42630.31920.9262-0.23960.40950.1443-0.03630.7203-0.06890.3869-11.6126-1.833514.2508
114.3649-0.16531.04892.7833-0.64411.8858-0.2563-0.6240.51190.15530.5277-0.6732-0.02051.3015-0.05650.2966-0.00130.03870.9116-0.2140.5848-4.34116.11869.7402
124.915-0.4846-3.47013.60541.07482.42460.0879-0.3841.5745-0.03310.5904-0.5723-0.78850.5737-0.34950.4462-0.16180.13220.4314-0.23760.9757-14.212915.18910.3243
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 700 through 717 )A700 - 717
2X-RAY DIFFRACTION2chain 'A' and (resid 718 through 739 )A718 - 739
3X-RAY DIFFRACTION3chain 'A' and (resid 740 through 756 )A740 - 756
4X-RAY DIFFRACTION4chain 'A' and (resid 757 through 830 )A757 - 830
5X-RAY DIFFRACTION5chain 'A' and (resid 831 through 928 )A831 - 928
6X-RAY DIFFRACTION6chain 'A' and (resid 929 through 984 )A929 - 984
7X-RAY DIFFRACTION7chain 'B' and (resid 699 through 731 )B699 - 731
8X-RAY DIFFRACTION8chain 'B' and (resid 732 through 767 )B732 - 767
9X-RAY DIFFRACTION9chain 'B' and (resid 768 through 830 )B768 - 830
10X-RAY DIFFRACTION10chain 'B' and (resid 831 through 892 )B831 - 892
11X-RAY DIFFRACTION11chain 'B' and (resid 893 through 928 )B893 - 928
12X-RAY DIFFRACTION12chain 'B' and (resid 929 through 984 )B929 - 984

+
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