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- EMDB-29497: Chimeric HsGATOR1-SpGtr-SpLam complex -

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Basic information

Entry
Database: EMDB / ID: EMD-29497
TitleChimeric HsGATOR1-SpGtr-SpLam complex
Map data
Sample
  • Complex: Chimeric HsGATOR1-SpGtr-SpLam complex
    • Protein or peptide: x 9 types
  • Ligand: x 3 types
KeywordsmTOR complex 1 (mTORC1) / Rag GTPase / Gtr GTPase / LAMTOR / GATOR1 / nutrient sensing / SIGNALING PROTEIN
Function / homology
Function and homology information


GATOR1 complex / aorta morphogenesis / TORC1 signaling / Amino acids regulate mTORC1 / cardiac muscle tissue development / negative regulation of TOR signaling / vacuolar membrane / ventricular septum development / negative regulation of kinase activity / roof of mouth development ...GATOR1 complex / aorta morphogenesis / TORC1 signaling / Amino acids regulate mTORC1 / cardiac muscle tissue development / negative regulation of TOR signaling / vacuolar membrane / ventricular septum development / negative regulation of kinase activity / roof of mouth development / positive regulation of autophagy / negative regulation of TORC1 signaling / cellular response to amino acid starvation / GTPase activator activity / small GTPase binding / lysosome / intracellular signal transduction / lysosomal membrane / protein-containing complex binding / perinuclear region of cytoplasm / cytosol
Similarity search - Function
: / Nitrogen permease regulator 3 / Nitrogen permease regulator 2 / Vacuolar membrane-associated protein Iml1 / DEPDC5 protein, C-terminal / Nitrogen Permease regulator of amino acid transport activity 3 / Nitrogen permease regulator 2 / Vacuolar membrane-associated protein Iml1, N-terminal domain / DEPDC5 protein C-terminal region / Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP) ...: / Nitrogen permease regulator 3 / Nitrogen permease regulator 2 / Vacuolar membrane-associated protein Iml1 / DEPDC5 protein, C-terminal / Nitrogen Permease regulator of amino acid transport activity 3 / Nitrogen permease regulator 2 / Vacuolar membrane-associated protein Iml1, N-terminal domain / DEPDC5 protein C-terminal region / Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP) / DEP domain profile. / Domain found in Dishevelled, Egl-10, and Pleckstrin / DEP domain / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
GATOR1 complex protein DEPDC5 / GATOR1 complex protein NPRL3 / GATOR1 complex protein NPRL2
Similarity search - Component
Biological speciesHomo sapiens (human) / Escherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.08 Å
AuthorsTettoni SD / Egri SB / Doxsey DD / Ouch C / Chang J / Song K / Xu C / Shen K
Funding support United States, 2 items
OrganizationGrant numberCountry
American Heart Association United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: Structure / Year: 2023
Title: Structure of the Schizosaccharomyces pombe Gtr-Lam complex reveals evolutionary divergence of mTORC1-dependent amino acid sensing.
Authors: Steven D Tettoni / Shawn B Egri / Dylan D Doxsey / Kristen Veinotte / Christna Ouch / Jeng-Yih Chang / Kangkang Song / Chen Xu / Kuang Shen /
Abstract: mTORC1 is a protein kinase complex that controls cellular growth in response to nutrient availability. Amino acid signals are transmitted toward mTORC1 via the Rag/Gtr GTPases and their upstream ...mTORC1 is a protein kinase complex that controls cellular growth in response to nutrient availability. Amino acid signals are transmitted toward mTORC1 via the Rag/Gtr GTPases and their upstream regulators. An important regulator is LAMTOR, which localizes Rag/Gtr on the lysosomal/vacuole membrane. In human cells, LAMTOR consists of five subunits, but in yeast, only three or four. Currently, it is not known how variation of the subunit stoichiometry may affect its structural organization and biochemical properties. Here, we report a 3.1 Å-resolution structural model of the Gtr-Lam complex in Schizosaccharomyces pombe. We found that SpGtr shares conserved architecture as HsRag, but the intersubunit communication that coordinates nucleotide loading on the two subunits differs. In contrast, SpLam contains distinctive structural features, but its GTP-specific GEF activity toward SpGtr is evolutionarily conserved. Our results revealed unique evolutionary paths of the protein components of the mTORC1 pathway.
History
DepositionJan 20, 2023-
Header (metadata) releaseJul 26, 2023-
Map releaseJul 26, 2023-
UpdateSep 20, 2023-
Current statusSep 20, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_29497.map.gz / Format: CCP4 / Size: 209.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.83 Å
Density
Contour LevelBy AUTHOR: 0.82
Minimum - Maximum-2.1298623 - 4.844037
Average (Standard dev.)0.009177184 (±0.1254188)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions380380380
Spacing380380380
CellA=B=C: 315.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_29497_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_29497_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Chimeric HsGATOR1-SpGtr-SpLam complex

EntireName: Chimeric HsGATOR1-SpGtr-SpLam complex
Components
  • Complex: Chimeric HsGATOR1-SpGtr-SpLam complex
    • Protein or peptide: GATOR complex protein DEPDC5
    • Protein or peptide: GATOR complex protein NPRL2
    • Protein or peptide: GATOR complex protein NPRL3
    • Protein or peptide: GTP-binding protein Gtr1
    • Protein or peptide: GTP-binding protein Gtr2
    • Protein or peptide: Schizosaccharomyces pombe LAM1, Human LAMTOR1 ortholog
    • Protein or peptide: Schizosaccharomyces pombe LAM2, Human LAMTOR2 ortholog
    • Protein or peptide: Schizosaccharomyces pombe LAM3, Human LAMTOR3 ortholog
    • Protein or peptide: Schizosaccharomyces pombe LAM4, Human LAMTOR5 ortholog
  • Ligand: GUANOSINE-5'-DIPHOSPHATE
  • Ligand: ALUMINUM FLUORIDEAluminium fluoride
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Chimeric HsGATOR1-SpGtr-SpLam complex

SupramoleculeName: Chimeric HsGATOR1-SpGtr-SpLam complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 420 KDa

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Macromolecule #1: GATOR complex protein DEPDC5

MacromoleculeName: GATOR complex protein DEPDC5 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 181.325828 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MRTTKVYKLV IHKKGFGGSD DELVVNPKVF PHIKLGDIVE IAHPNDEYSP LLLQVKSLKE DLQKETISVD QTVTQVFRLR PYQDVYVNV VDPKDVTLDL VELTFKDQYI GRGDMWRLKK SLVSTCAYIT QKVEFAGIRA QAGELWVKNE KVMCGYISED T RVVFRSTS ...String:
MRTTKVYKLV IHKKGFGGSD DELVVNPKVF PHIKLGDIVE IAHPNDEYSP LLLQVKSLKE DLQKETISVD QTVTQVFRLR PYQDVYVNV VDPKDVTLDL VELTFKDQYI GRGDMWRLKK SLVSTCAYIT QKVEFAGIRA QAGELWVKNE KVMCGYISED T RVVFRSTS AMVYIFIQMS CEMWDFDIYG DLYFEKAVNG FLADLFTKWK EKNCSHEVTV VLFSRTFYDA KSVDEFPEIN RA SIRQDHK GRFYEDFYKV VVQNERREEW TSLLVTIKKL FIQYPVLVRL EQAEGFPQGD NSTSAQGNYL EAINLSFNVF DKH YINRNF DRTGQMSVVI TPGVGVFEVD RLLMILTKQR MIDNGIGVDL VCMGEQPLHA VPLFKLHNRS APRDSRLGDD YNIP HWINH SFYTSKSQLF CNSFTPRIKL AGKKPASEKA KNGRDTSLGS PKESENALPI QVDYDAYDAQ VFRLPGPSRA QCLTT CRSV RERESHSRKS ASSCDVSSSP SLPSRTLPTE EVRSQASDDS SLGKSANILM IPHPHLHQYE VSSSLGYTST RDVLEN MME PPQRDSSAPG RFHVGSAESM LHVRPGGYTP QRALINPFAP SRMPMKLTSN RRRWMHTFPV GPSGEAIQIH HQTRQNM AE LQGSGQRDPT HSSAELLELA YHEAAGRHSN SPQPGDGMSF LNFSGTEELS VGLLSNSGAG MNPRTQNKDS LEDSVSTS P DPILTLSAPP VVPGFCCTVG VDWKSLTTPA CLPLTTDYFP DRQGLQNDYT EGCADLLPEA DIDRRDEDGV QMTAQQVFE EFICQRLMQG YQIIVQPKTQ KPNPAVPPPL SSSPLYSRGL VSRNRPEEED QYWLSMGRTF HKVTLKDKMI TVTRYLPKYP YESAQIHYT YSLCPSHSDS EFVSCWVEFS HERLEEYKWN YLDQYICSAG SEDFSLIESL KFWRTRFLLL PACVTATKRI T EGEAHCDI YGDRPRADED EWQLLDGFVR FVEGLNRIRR RHRSDRMMRK GTAMKGLQMT GPISTHSLES TAPPVGKKGT SA LSALLEM EASQKCLGEQ QAAVHGGKSS AQSAESSSVA MTPTYMDSPR KDGAFFMEFV RSPRTASSAF YPQVSVDQTA TPM LDGTSL GICTGQSMDR GNSQTFGNSQ NIGEQGYSST NSSDSSSQQL VASSLTSSST LTEILEAMKH PSTGVQLLSE QKGL SPYCF ISAEVVHWLV NHVEGIQTQA MAIDIMQKML EEQLITHASG EAWRTFIYGF YFYKIVTDKE PDRVAMQQPA TTWHT AGVD DFASFQRKWF EVAFVAEELV HSEIPAFLLP WLPSRPASYA SRHSSFSRSF GGRSQAAALL AATVPEQRTV TLDVDV NNR TDRLEWCSCY YHGNFSLNAA FEIKLHWMAV TAAVLFEMVQ GWHRKATSCG FLLVPVLEGP FALPSYLYGD PLRAQLF IP LNISCLLKEG SEHLFDSFEP ETYWDRMHLF QEAIAHRFGF VQDKYSASAF NFPAENKPQY IHVTGTVFLQ LPYSKRKF S GQQRRRRNST SSTNQNMFCE ERVGYNWAYN TMLTKTWRSS ATGDEKFADR LLKDFTDFCI NRDNRLVTFW TSCLEKMHA SAP

UniProtKB: GATOR1 complex protein DEPDC5

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Macromolecule #2: GATOR complex protein NPRL2

MacromoleculeName: GATOR complex protein NPRL2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 45.799547 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGYPYDVPDY ADLNGGGGGS TMGSGCRIEC IFFSEFHPTL GPKITYQVPE DFISRELFDT VQVYIITKPE LQNKLITVTA MEKKLIGCP VCIEHKKYSR NALLFNLGFV CDAQAKTCAL EPIVKKLAGY LTTLELESSF VSMEESKQKL VPIMTILLEE L NASGRCTL ...String:
MGYPYDVPDY ADLNGGGGGS TMGSGCRIEC IFFSEFHPTL GPKITYQVPE DFISRELFDT VQVYIITKPE LQNKLITVTA MEKKLIGCP VCIEHKKYSR NALLFNLGFV CDAQAKTCAL EPIVKKLAGY LTTLELESSF VSMEESKQKL VPIMTILLEE L NASGRCTL PIDESNTIHL KVIEQRPDPP VAQEYDVPVF TKDKEDFFNS QWDLTTQQIL PYIDGFRHIQ KISAEADVEL NL VRIAIQN LLYYGVVTLV SILQYSNVYC PTPKVQDLVD DKSLQEACLS YVTKQGHKRA SLRDVFQLYC SLSPGTTVRD LIG RHPQQL QHVDERKLIQ FGLMKNLIRR LQKYPVRVTR EEQSHPARLY TGCHSYDEIC CKTGMSYHEL DERLENDPNI IICW K

UniProtKB: GATOR1 complex protein NPRL2

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Macromolecule #3: GATOR complex protein NPRL3

MacromoleculeName: GATOR complex protein NPRL3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 65.769 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGYPYDVPDY ADLNGGGGGS TMRDNTSPIS VILVSSGSRG NKLLFRYPFQ RSQEHPASQT SKPRSRYAAS NTGDHADEQD GDSRFSDVI LATILATKSE MCGQKFELKI DNVRFVGHPT LLQHALGQIS KTDPSPKREA PTMILFNVVF ALRANADPSV I NCLHNLSR ...String:
MGYPYDVPDY ADLNGGGGGS TMRDNTSPIS VILVSSGSRG NKLLFRYPFQ RSQEHPASQT SKPRSRYAAS NTGDHADEQD GDSRFSDVI LATILATKSE MCGQKFELKI DNVRFVGHPT LLQHALGQIS KTDPSPKREA PTMILFNVVF ALRANADPSV I NCLHNLSR RIATVLQHEE RRCQYLTREA KLILALQDEV SAMADGNEGP QSPFHHILPK CKLARDLKEA YDSLCTSGVV RL HINSWLE VSFCLPHKIH YAASSLIPPE AIERSLKAIR PYHALLLLSD EKSLLGELPI DCSPALVRVI KTTSAVKNLQ QLA QDADLA LLQVFQLAAH LVYWGKAIII YPLCENNVYM LSPNASVCLY SPLAEQFSHQ FPSHDLPSVL AKFSLPVSLS EFRN PLAPA VQETQLIQMV VWMLQRRLLI QLHTYVCLMA SPSEEEPRPR EDDVPFTARV GGRSLSTPNA LSFGSPTSSD DMTLT SPSM DNSSAELLPS GDSPLNQRMT ENLLASLSEH ERAAILSVPA AQNPEDLRMF ARLLHYFRGR HHLEEIMYNE NTRRSQ LLM LFDKFRSVLV VTTHEDPVIA VFQALLP

UniProtKB: GATOR1 complex protein NPRL3

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Macromolecule #4: GTP-binding protein Gtr1

MacromoleculeName: GTP-binding protein Gtr1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 36.500449 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MRKKVLLMGR SGSGKSSMRS IVFSNYVAKD TRRLGATIDI EHSHVRFLGN LVLNLWDCGG QEAFMENYLS AQRDHIFRNV QVLIYVFDV ESREFERDLV TFRNCLEATV ANSPQARVFC LIHKMDLVQE DLRDLVFEER KAILLETSKD LETTCLATSI W DETLFKAW ...String:
MRKKVLLMGR SGSGKSSMRS IVFSNYVAKD TRRLGATIDI EHSHVRFLGN LVLNLWDCGG QEAFMENYLS AQRDHIFRNV QVLIYVFDV ESREFERDLV TFRNCLEATV ANSPQARVFC LIHKMDLVQE DLRDLVFEER KAILLETSKD LETTCLATSI W DETLFKAW SAIVYTLIPN TPTLESHLRE FAKAAEAAEV ILFERTTFLV ISSYSSESNP ATDAHRFEKI SNIVKQFKLS CS KMQAQFT TFELRGGNFS AFIVPYTEDT YILVVIADPE IESAVTLMNI QSARRFIEAS KSASDGIQLQ PGSGGSHHHH HHH H

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Macromolecule #5: GTP-binding protein Gtr2

MacromoleculeName: GTP-binding protein Gtr2 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 35.547559 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MKPRKIILMG LRRSGKSSIQ KVVFYKMPPN ETLALESTSK LTQDHISSFI DFSVWDFPGQ VDVFDAAFDF ESIFTQVGAL IFVIDAQDD YLDALARLHV TVARVVTINP NICIEVFIHK VDGLSDEFKI DTQRDIQQRT QDELADIGLE NVPISFHLTS I FDHSIFEA ...String:
MKPRKIILMG LRRSGKSSIQ KVVFYKMPPN ETLALESTSK LTQDHISSFI DFSVWDFPGQ VDVFDAAFDF ESIFTQVGAL IFVIDAQDD YLDALARLHV TVARVVTINP NICIEVFIHK VDGLSDEFKI DTQRDIQQRT QDELADIGLE NVPISFHLTS I FDHSIFEA FSRVIQKLIP QLPTLENLLN IFCSNSLVEK AYLFDVLSKI YVATDSSPVD VQSYEICSDF IDVILDIGSI YG RSSQLKP GHSPEILDET SSVIRLSNDL VLFLREMNQY LALICIVRAD NFEKSGLIEY NVQCLQTAIQ SIFSPRT

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Macromolecule #6: Schizosaccharomyces pombe LAM1, Human LAMTOR1 ortholog

MacromoleculeName: Schizosaccharomyces pombe LAM1, Human LAMTOR1 ortholog
type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 43.686832 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKER AEISMLEGAV LDIRYGVSRI AYSKDFETLK VDFLSKLPEM LKMFEDRLCH KTYLNGDHVT HPDFMLYDAL D VVLYMDPM ...String:
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKER AEISMLEGAV LDIRYGVSRI AYSKDFETLK VDFLSKLPEM LKMFEDRLCH KTYLNGDHVT HPDFMLYDAL D VVLYMDPM CLDAFPKLVC FKKRIEAIPQ IDKYLKSSKY IAWPLQGWQA TFGGGDHPPK SDLVPRGSPN SSFLFNNSDD ID EQTPLLN NDGIQRTPPS AEADMSLRKR EEEEEWESKV YDVAKNKFID VFSLRLRTEA PQRDPRDNIY EEVLDQIDSL NLD PKYDVA KPTEQETEFI IRKLGVLIDD INNIKLSDKE IKGKMVINLS KVQPNITGSP S

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Macromolecule #7: Schizosaccharomyces pombe LAM2, Human LAMTOR2 ortholog

MacromoleculeName: Schizosaccharomyces pombe LAM2, Human LAMTOR2 ortholog
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 19.830908 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGSSHHHHHH SLEVLFQGPG SMIKPKKLSS LMKQAVEETV PSIMVFTTTG SLLAYVSFED PKDGLKRLDL AKRVRSIAAL AGNMYSLYT ATNPSPLVAE STDDVIAHQR DVLFETIIEF ERGKLLIAAI SIDGAEDKLY SKDPLLLGIV GTENAKEGMM Q IKSELLKE CITNELSTLG KPV

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Macromolecule #8: Schizosaccharomyces pombe LAM3, Human LAMTOR3 ortholog

MacromoleculeName: Schizosaccharomyces pombe LAM3, Human LAMTOR3 ortholog
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 12.707468 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSVSQQLSEL ASKEKTVLYV ADQNLEEVLC FPESTDRTTL VQLTDACLHA NELAKHLEFG KPLSITNQYS RGSCVLQIAK EKKDGSGMV VSTTIAAHNA LRGALKCSNA LDQVISQL

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Macromolecule #9: Schizosaccharomyces pombe LAM4, Human LAMTOR5 ortholog

MacromoleculeName: Schizosaccharomyces pombe LAM4, Human LAMTOR5 ortholog
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 8.984198 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MDSQLSENLL KCVNETYRGA MLVRNGLPIA TAGDVNAEEQ RVICEWNSNA VSEVLHLHDS NTKILIATKE SCVLGLIYRN T

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Macromolecule #10: GUANOSINE-5'-DIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-DIPHOSPHATE / type: ligand / ID: 10 / Number of copies: 2 / Formula: GDP
Molecular weightTheoretical: 443.201 Da
Chemical component information

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

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Macromolecule #11: ALUMINUM FLUORIDE

MacromoleculeName: ALUMINUM FLUORIDE / type: ligand / ID: 11 / Number of copies: 1 / Formula: AF3
Molecular weightTheoretical: 83.977 Da
Chemical component information

ChemComp-AF3:
ALUMINUM FLUORIDE / Aluminium fluoride

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Macromolecule #12: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 12 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.7 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.08 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 659887

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