[English] 日本語
Yorodumi
- EMDB-43299: Structure of mouse RyR1 in complex with S100A1 (EGTA-only dataset) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-43299
TitleStructure of mouse RyR1 in complex with S100A1 (EGTA-only dataset)
Map dataRyR1 with S100A1, EGTA
Sample
  • Complex: Complex of RyR1 with Calstabin-1 and S100A1 (EGTA condition)
    • Protein or peptide: Ryanodine receptor 1
    • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1A
    • Protein or peptide: Protein S100A1
  • Ligand: ZINC ION
  • Ligand: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
KeywordsCalcium / Ion Channel / MEMBRANE PROTEIN
Function / homology
Function and homology information


junctional membrane complex / TGF-beta receptor signaling activates SMADs / Calcineurin activates NFAT / mTORC1-mediated signalling / regulation of response to osmotic stress / regulation of muscle contraction / sarcoplasmic reticulum calcium ion transport / cytoplasmic side of membrane / transforming growth factor beta receptor binding / Stimuli-sensing channels ...junctional membrane complex / TGF-beta receptor signaling activates SMADs / Calcineurin activates NFAT / mTORC1-mediated signalling / regulation of response to osmotic stress / regulation of muscle contraction / sarcoplasmic reticulum calcium ion transport / cytoplasmic side of membrane / transforming growth factor beta receptor binding / Stimuli-sensing channels / Ion homeostasis / type I transforming growth factor beta receptor binding / heart trabecula formation / S100 protein binding / terminal cisterna / ryanodine receptor complex / ryanodine-sensitive calcium-release channel activity / response to caffeine / release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / ventricular cardiac muscle tissue morphogenesis / ossification involved in bone maturation / cellular response to ATP / regulation of heart contraction / skin development / FK506 binding / organelle membrane / positive regulation of sprouting angiogenesis / cellular response to caffeine / extrinsic component of cytoplasmic side of plasma membrane / outflow tract morphogenesis / regulation of ryanodine-sensitive calcium-release channel activity / voltage-gated calcium channel activity / smooth endoplasmic reticulum / heart morphogenesis / skeletal muscle fiber development / striated muscle contraction / T cell proliferation / axon terminus / release of sequestered calcium ion into cytosol / muscle contraction / regulation of cytosolic calcium ion concentration / calcium channel complex / T-tubule / sarcoplasmic reticulum membrane / Hsp70 protein binding / sarcomere / cellular response to calcium ion / sarcoplasmic reticulum / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / negative regulation of transforming growth factor beta receptor signaling pathway / calcium channel activity / sarcolemma / cytokine-mediated signaling pathway / Z disc / cytoplasmic side of plasma membrane / calcium ion transport / ATPase binding / protease binding / protein homotetramerization / vesicle / transmembrane transporter binding / calmodulin binding / calcium ion binding / synapse / perinuclear region of cytoplasm / Golgi apparatus / enzyme binding / protein homodimerization activity / protein-containing complex / mitochondrion / nucleoplasm / ATP binding / identical protein binding / membrane / cytosol / cytoplasm
Similarity search - Function
Protein S100-A1 / S-100/ICaBP type calcium binding protein signature. / S100/Calcium binding protein 7/8-like, conserved site / S100/CaBP-9k-type, calcium binding, subdomain / S-100/ICaBP type calcium binding domain / S-100/ICaBP type calcium binding domain / EF hand / Ryanodine receptor, SPRY domain 2 / : / Ryanodine receptor junctional solenoid repeat ...Protein S100-A1 / S-100/ICaBP type calcium binding protein signature. / S100/Calcium binding protein 7/8-like, conserved site / S100/CaBP-9k-type, calcium binding, subdomain / S-100/ICaBP type calcium binding domain / S-100/ICaBP type calcium binding domain / EF hand / Ryanodine receptor, SPRY domain 2 / : / Ryanodine receptor junctional solenoid repeat / Ryanodine Receptor TM 4-6 / Ryanodine receptor / Ryanodine receptor, SPRY domain 1 / Ryanodine receptor, SPRY domain 3 / Ryanodine Receptor TM 4-6 / Ryanodine receptor Ryr / RyR domain / RyR/IP3 receptor binding core, RIH domain superfamily / RyR/IP3R Homology associated domain / Inositol 1,4,5-trisphosphate/ryanodine receptor / RIH domain / RyR and IP3R Homology associated / Inositol 1,4,5-trisphosphate/ryanodine receptor / RIH domain / : / : / MIR motif / MIR domain / MIR domain profile. / Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases / Mir domain superfamily / SPRY domain / B30.2/SPRY domain / B30.2/SPRY domain profile. / B30.2/SPRY domain superfamily / Domain in SPla and the RYanodine Receptor. / SPRY domain / FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / FKBP-type peptidyl-prolyl cis-trans isomerase domain / FKBP-type peptidyl-prolyl cis-trans isomerase / Peptidyl-prolyl cis-trans isomerase domain superfamily / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / Ion transport domain / Ion transport protein / EF-hand domain pair / Concanavalin A-like lectin/glucanase domain superfamily
Similarity search - Domain/homology
Ryanodine receptor 1 / Peptidyl-prolyl cis-trans isomerase FKBP1A / Protein S100
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.21 Å
AuthorsWeninger G / Marks AR
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)R01HL145473 United States
CitationJournal: Proc Natl Acad Sci U S A / Year: 2024
Title: Structural insights into the regulation of RyR1 by S100A1.
Authors: Gunnar Weninger / Marco C Miotto / Carl Tchagou / Steven Reiken / Haikel Dridi / Sören Brandenburg / Gabriel C Riedemann / Qi Yuan / Yang Liu / Alexander Chang / Anetta Wronska / Stephan E ...Authors: Gunnar Weninger / Marco C Miotto / Carl Tchagou / Steven Reiken / Haikel Dridi / Sören Brandenburg / Gabriel C Riedemann / Qi Yuan / Yang Liu / Alexander Chang / Anetta Wronska / Stephan E Lehnart / Andrew R Marks /
Abstract: S100A1, a small homodimeric EF-hand Ca-binding protein (~21 kDa), plays an important regulatory role in Ca signaling pathways involved in various biological functions including Ca cycling and ...S100A1, a small homodimeric EF-hand Ca-binding protein (~21 kDa), plays an important regulatory role in Ca signaling pathways involved in various biological functions including Ca cycling and contractile performance in skeletal and cardiac myocytes. One key target of the S100A1 interactome is the ryanodine receptor (RyR), a huge homotetrameric Ca release channel (~2.3 MDa) of the sarcoplasmic reticulum. Here, we report cryoelectron microscopy structures of S100A1 bound to RyR1, the skeletal muscle isoform, in absence and presence of Ca. Ca-free apo-S100A1 binds beneath the bridging solenoid (BSol) and forms contacts with the junctional solenoid and the shell-core linker of RyR1. Upon Ca-binding, S100A1 undergoes a conformational change resulting in the exposure of the hydrophobic pocket known to serve as a major interaction site of S100A1. Through interactions of the hydrophobic pocket with RyR1, Ca-bound S100A1 intrudes deeper into the RyR1 structure beneath BSol than the apo-form and induces sideways motions of the C-terminal BSol region toward the adjacent RyR1 protomer resulting in tighter interprotomer contacts. Interestingly, the second hydrophobic pocket of the S100A1-dimer is largely exposed at the hydrophilic surface making it prone to interactions with the local environment, suggesting that S100A1 could be involved in forming larger heterocomplexes of RyRs with other protein partners. Since S100A1 interactions stabilizing BSol are implicated in the regulation of RyR-mediated Ca release, the characterization of the S100A1 binding site conserved between RyR isoforms may provide the structural basis for the development of therapeutic strategies regarding treatments of RyR-related disorders.
History
DepositionJan 8, 2024-
Header (metadata) releaseJan 24, 2024-
Map releaseJan 24, 2024-
UpdateOct 16, 2024-
Current statusOct 16, 2024Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

emd_43299.png

Downloads & links

-
Map

FileDownload / File: emd_43299.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationRyR1 with S100A1, EGTA
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 512 pix.
= 428.544 Å		0.84 Å/pix.
x 512 pix.
= 428.544 Å		0.84 Å/pix.
x 512 pix.
= 428.544 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.837 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum0.0 - 0.68600434
Average (Standard dev.)0.003779209 (±0.026466217)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 428.544 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Sample components

-
Entire : Complex of RyR1 with Calstabin-1 and S100A1 (EGTA condition)

EntireName: Complex of RyR1 with Calstabin-1 and S100A1 (EGTA condition)
Components
  • Complex: Complex of RyR1 with Calstabin-1 and S100A1 (EGTA condition)
    • Protein or peptide: Ryanodine receptor 1
    • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1A
    • Protein or peptide: Protein S100A1
  • Ligand: ZINC ION
  • Ligand: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE

-
Supramolecule #1: Complex of RyR1 with Calstabin-1 and S100A1 (EGTA condition)

SupramoleculeName: Complex of RyR1 with Calstabin-1 and S100A1 (EGTA condition)
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Mus musculus (house mouse)

-
Macromolecule #1: Ryanodine receptor 1

MacromoleculeName: Ryanodine receptor 1 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 565.692562 KDa
SequenceString: MGDGGGEGED EVQFLRTDDE VVLQCSATVL KEQLKLCLAA EGFGNRLCFL EPTSNAQNVP PDLAICCFIL EQSLSVRALQ EMLANTVEA GVESSQGGGH RTLLYGHAIL LRHAHSRMYL SCLTTSRSMT DKLAFDVGLQ EDATGEACWW TMHPASKQRS E GEKVRVGD ...String:
MGDGGGEGED EVQFLRTDDE VVLQCSATVL KEQLKLCLAA EGFGNRLCFL EPTSNAQNVP PDLAICCFIL EQSLSVRALQ EMLANTVEA GVESSQGGGH RTLLYGHAIL LRHAHSRMYL SCLTTSRSMT DKLAFDVGLQ EDATGEACWW TMHPASKQRS E GEKVRVGD DLILVSVSSE RYLHLSTASG ELQVDASFMQ TLWNMNPICS GCEEGFVTGG HVLRLFHGHM DECLTISPSD SD DQRRLVY YEGGPVCTHA RSLWRLEPLR ISWSGSHLRW GQPLRIRHVT TGRYLGLTED QGLVVVDASK AHTKATSFCF RIS KEKLDV APKRDVEGMG PPEIKYGESL CFVQHVASGL WLTYAAPDPK ALRLGVLKKK AMLHQEGHMD DALSLTRCQQ EESQ AARMI YSTAGLYNQF IKGLDSFSGK PRGSGPPAGS ALPIEGVILS LQDLIGYFEP PSEELQHEEK QTKLRSLRNR QSLFQ EEGM LSLVLNCIDR LNVYTTAAHF AEFAGEEAAE SWKEIVNLLY ELLASLIRGN RTNCALFSTN LDWLVSKLDR LEASSG ILE VLYCVLIESP EVLNIIQENH IKSIISLLDK HGRNHKVLDV LCSLCVCNGV AVRSNQDLIT ENLLPGRELL LQTNLIN YV TSIRPNIFVG RAEGSTQYGK WYFEVMVDEV APFLTAQATH LRVGWALSEG YSPYPGGGEG WGGNGVGDDL YSYGFDGL H LWTGHVARPV TSPGQHLLAP EDVVSCCLDL SVPSISFRIN GCPVQGVFES FNLDGLFFPV VSFSAGIKVR FLLGGRHGE FKFLPPPGYA PCHEAVLPRE RLHLQPIKEY RREGPRGPHL VGPSRCLSHL DFVPCPVDTI QIVLPPHLER IREKLAENIH ELWALTRIE QGWTYGPVRD DNKRLHPCLV NFHSLPEPER NYNLQMSGET LKTLLALGCH VGMADEKAED NLKKTKLPKT Y MMSNGYKP APLDLSHVRL TPAQTTLVDR LAENGHNVWA RDRVAQGWSY SAVQDIPARR NPRLVPYRLL DEATKRSNRD SL CQAVRTL LGYGYNIEPP DQEPSQVDSQ SRGDRARIFR AEKSYAVQSG RWYFEFEAVT TGEMRVGWAR PELRPDVELG ADD LAYVFN GHRGQRWHLG SEPFGRPWQS GDVVGCMIDL TENTIIFTLN GEVLMSDSGS ETAFRDIEIG DGFLPVCSLG PGQV GHLNL GQDVSSLRFF AICGLQEGFE PFAINMQRPV TTWFSKSLPQ FEPVPLEHPH YEVARMDGTV DTPPCLRLTH RTWGS QNSL VEMLFLRLSL PVQFHQHFRC TAGATPLASP GLQPPAEDEA RAAEPDTDYE NLRRSAGGWG EAEGGKDGTA KEGTPG GTA QAGVEAQPAR AENEKDATTE KNKKRGFLFK AKKVAMMTQP PSTPALPRLP RDVVPADNRD DPEIILNTTT YYYSVRV FA GQEPSCVWVG WVTPDYHQHD MSFDLSKVRA VTVTMGDEQG NVHSSLKCSN CYMVWGGDFV SPGQQGRISH TDLVIGCL V DLATGLMTFT ANGKESNTFF QVEPNTKLFP AVFVLPTHQN VVQFELGKQK NIMPLSAAMF LSERKNPAPQ CPPRLEVQM LMPVSWSRMP NHFLQVDTRR AGERLGWAVQ CQEPLMMMAL HIPEENRCMD ILELSERLDL QRFHSHTLSL YRSVCALGNN RVAHALCSH VDQAQLLHAL EDARLPGPLR AGYYDLLISI HLESACRSRR SMLSEYIVPL TPETRAITLF PPGRSAEDGP R RHGLPGVG VTTSLRPPHH FSPPCFVVAL PAAGATEAPA RLSPAIPLEA LRDKALRMLG EAVRDGGQHA RDPVGGSVEF QF VPVLKLV STLLVMGVFS DEDVKQILKM IEPEVFREEE EVEEEGEEEE EDEEEKEEDE EEEAHEKEDE EKEEAEDAAE EEK EELEEG LLQMKLPESV KLQMCHLLEY FCDQELQHRV ESLAAFAECY VDKMQGNQRG RYGLLMKAFT MSAAETARRT REFR SPPQE QINMLLHFKN GADEEECPLP EEIRQELVNF HQDLLAHCGI QLEGEEEEPE EESTLGSRLM SLLEKVKLVK KTEEK PEEE PAPEEHKPQS LQELVSHTVV RWAQEDFVQS PELVRAMFSL LHRQYDGLGE LLRALPRAYT ISVSSVEDTM SLLECL GQI RSLLIVQMGP QEENLMIQSI GNIMNNKVFY QHPNLMRALG MHETVMEVMV NVLGGGESKE IRFPKMVTSC CRFLCYF CR ISRQNQRSMF DHLSYLLENS GIGLGMQGST PLDVAAASVI DNNELALALQ EQDLEKVVSY LAGCGLQSCP MLLAKGYP D IGWNPCGGER YLDFLRFAVF VNGESVEENA NVVVRLLIRK PECFGPALRG EGGSGLLAAI EEAIRISEDP ARDGPGVRR DRRREHFGEE PPEENRVHLG HAIMSFYAAL IDLLGRCAPE THLIQAGKGE ALRIRAILRS LVPLDDLVGI ISLPLQIPTL GKDGALVQP KMSASFVPDH KASMVLFLDR VYGIENQDFL LHVLDVGFLP DMRAAASLDT ATFSTTEMAL ALNRYLCLAV L PLITKCAP LFAGTEHRAI MVDSMLHTVY RLSRGRSLTK AQRDVIEDCL MALCRYIRPS MLQHLLRRLV FDVPILNEFA KM PLKLLTN HYERCWKYYC LPTGWANFGV TSEEELHLTR KLFWGIFDSL AHKKYDQELY RIAMPCLCAI AGALPPDYVD ASY SSKTEK KATVDAEGNF DPRPVETLNV IIPEKLDSFI NKFAEYTHEK WAFDKIQNNW SYGENIDEEL KTHPMLRPYK TFSE KDKEI YRWPIKESLK AMIAWEWTVE KAREGEEEKT EKKKTRKISQ TAQTYDPREG YNPQPPDLSV VTLSRELQAM AEQLA ENYH NTWGRKKKQE LEAKGGGSHP LLVPYDTLTA KEKARDREKA QELLKFLQMN GYAVTRGLKD MELDTSSIEK RFAFGF LQQ LLRWMDISQE FIAHLEAVVS SGRVEKSPHE QEIKFFAKIL LPLINQYFTN HCLYFLSTPA KVLGSGGHAS NKEKEMI TS LFCKLAALVR HRVSLFGTDA PAVVNCLHIL ARSLDARTVM KSGPEIVKAG LRSFFESASE DIEKMVENLR LGKVSQAR T QVKGVGQNLT YTTVALLPVL TTLFQHIAQH QFGDDVILDD VQVSCYRTLC SIYSLGTTRN PYVEKLRPAL GECLARLAA AMPVAFLEPE LNEYNACSVY TTKSPRERAI LGLPNSVEEM CPDIPVLERL MAEIGGLAES GARYTEMPHV IEITLPMLCS YLPRWWERG PEAPPPALPA GAPPPCTAVT SDHLNSLLGN ILRIIVNNLG IDEASWMKRL AVFAQPIVSR ARPELLRSHF I PTIGRLRK RAGKVVAEEE QLRLEAKAEA EEGELLVRDE FSVLCRDLYA LYPLLIRYVD NNRAHWLTEP NPNAEELFRM VG EIFIYWS KSHNFKREEQ NFVVQNEINN MSFLTADNKS KMAKAGDVQS GGSDQERTKK KRRGDRYSVQ TSLIVATLKK MLP IGLNMC APTDQDLIVL AKARYALKDT DEEVREFLQN NLNLQGKVEG SPSLRWQMAL YRGVPGREED ADDPEKIVRR VQEV SAVLY HLDQTEHPYK SKKAVWHKLL SKQRRRAVVA CFRMTPLYNL PTHRACNMFL ESYKASWILT EDHSFEDRMI DDLSK AGEQ EEEEEEVEEK KPDPLHQLVL HFSRTALTEK SKLDEDYLYM AYADIMAKSC HLEEGGENGE EGGEEEEVEV SFEEKE MEK QRLLYQQSRL HNRGAAEMVL QMISACKGET GAMVSSTLKL GISILNGGNA EVQQKMLDYL KDKKEVGFFQ SIQALMQ TC SVLDLNAFER QNKAEGLGMV NEDGTVINRQ NGEKVMADDE FTQDLFRFLQ LLCEGHNNDF QNYLRTQTGN TTTINIII C TVDYLLRLQE SISDFYWYYS GKDVIEEQGK RNFSKAMSVA KQVFNSLTEY IQGPCTGNQQ SLAHSRLWDA VVGFLHVFA HMMMKLAQDS SQIELLKELL DLQKDMVVML LSLLEGNVVN GMIARQMVDM LVESSSNVEM ILKFFDMFLK LKDIVGSEAF QDYVTDPRG LISKKDFQKA MDSQKQFTGP EIQFLLSCSE ADENEMINCE EFANRFQEPA RDIGFNVAVL LTNLSEHVPH D PRLRNFLE LAESILEYFR PYLGRIEIMG ASRRIERIYF EISETNRAQW EMPQVKESKR QFIFDVVNEG GESEKMEMFV SF CEDTIFE MQIAAQISEP EGEPEEDEDE GAEEAEEGAA GSDGSGSAAA AGVWVWLAAT AGRTLRGLSY RSLRRRVRRL RRL TAREAA TAVAALLWAL VTRAGGAGAG AAAGALRLLW GSLFGGGLVD SAKKVTVTEL LAGMPDPTGD EVHGQQPSGA GSDA EGEGE GEGEGDAADG AGDEEAAADQ AGTGGADGAV AVADGSPFRP EGAGGLGDMG DTTPVEPPTP EGSPILKRKL GVDGE EEEP PPEPEPEPEP EPEKADTENG EKEVPEPPPE PPKKTPPPPP PKKEEAGGAG LEEFWGELEV QRVKFLNYLS RNFYTL RFL ALFLAFAINF ILLFYKVSDS PPGEDDIEGS GAGDMSGAGS GDGSGWGSRA GEEVEGDEDE NMVYYFLEES TGYMEPA LR CLSLLHTLVA FLCIIGYNCL KVPLVIFKRE KELARKLEFD GLYITEQPED DDVKGQWDRL VLNTPSFPSN YWDKFVKR K VLDKHGDIFG RERIAELLGM DLASLEITAH NERKPDPPPG LLTWIMSIDV KYQIWKFGVI FTDNSFLYLG WYMVMSLLG HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYLYT VVAFNFFRKF YNKSEDEDEP DMKCDDMMTC YLFHMYVGV RAGGGIGDEI EDPAGDEYEL YRVVFDITFF FFVIVILLAI IQGLIIDAFG ELRDQQEQVK EDMETKCFIC G IGSDYFDT TPHGFETHTL EEHNLANYMF FLMYLINKDE TEHTGQESYV WKMYQERCWD FFPAGDCFRK QYEDQLS

UniProtKB: Ryanodine receptor 1

-
Macromolecule #2: Peptidyl-prolyl cis-trans isomerase FKBP1A

MacromoleculeName: Peptidyl-prolyl cis-trans isomerase FKBP1A / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 11.939629 KDa
SequenceString:
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFT LGKQEVIRGW EEGVAQMSVG QRAKLIISSD YAYGATGHP GIIPPHATLV FDVELLKLE

UniProtKB: Peptidyl-prolyl cis-trans isomerase FKBP1A

-
Macromolecule #3: Protein S100A1

MacromoleculeName: Protein S100A1 / type: protein_or_peptide / ID: 3 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 10.516784 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGSELESAME TLINVFHAHS GKEGDKYKLS KKELKDLLQT ELSGFLDVQK DADAVDKVMK ELDENGDGEV DFKEYVVLVA ALTVACNNF FWETS

UniProtKB: Protein S100

-
Macromolecule #4: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 4 / Number of copies: 4 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

-
Macromolecule #5: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 5 / Number of copies: 8 / Formula: PCW
Molecular weightTheoretical: 787.121 Da
Chemical component information

ChemComp-PCW:
1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DOPC, phospholipid*YM

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration8.5 mg/mL
BufferpH: 7.4
Component:
ConcentrationNameFormula
10.0 mmol/LHEPES
150.0 mmol/Lsodium chlorideNaCl
0.25 %CHAPS
0.01 %DOPC
0.5 mmol/LTCEP
5.0 mmol/LEGTA
GridModel: Quantifoil R0.6/1 / Material: GOLD / Mesh: 300
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV
Details0.15 mmol/L S100A1-dimer

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Number real images: 12147 / Average electron dose: 58.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.2 µm / Nominal defocus min: 0.5 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: INSILICO MODEL / In silico model: CryoSPARC ab initio
Final reconstructionApplied symmetry - Point group: C4 (4 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.21 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 36506
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC / Details: CryoSPARC branch-and-bound
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC / Details: CryoSPARC branch-and-bound

+
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