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- EMDB-21513: Pig Ryanodine Receptor (WT) in 5mM EGTA condition -

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Basic information

Entry
Database: EMDB / ID: EMD-21513
TitlePig Ryanodine Receptor (WT) in 5mM EGTA condition
Map dataFinal map from cryoSPARC
Sample
  • Complex: ryanodine receptor-FKBP1B complex
    • Complex: ryanodine receptor
      • Protein or peptide: Ryanodine Receptor
    • Complex: FKBP1B
      • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1B
  • Ligand: ZINC ION
Keywordsreceptor / calcium / channel / complex / TRANSPORT PROTEIN-ISOMERASE complex
Function / homology
Function and homology information


positive regulation of sequestering of calcium ion / cyclic nucleotide binding / negative regulation of release of sequestered calcium ion into cytosol / negative regulation of insulin secretion involved in cellular response to glucose stimulus / neuronal action potential propagation / insulin secretion involved in cellular response to glucose stimulus / cell communication by electrical coupling involved in cardiac conduction / response to redox state / protein maturation by protein folding / 'de novo' protein folding ...positive regulation of sequestering of calcium ion / cyclic nucleotide binding / negative regulation of release of sequestered calcium ion into cytosol / negative regulation of insulin secretion involved in cellular response to glucose stimulus / neuronal action potential propagation / insulin secretion involved in cellular response to glucose stimulus / cell communication by electrical coupling involved in cardiac conduction / response to redox state / protein maturation by protein folding / 'de novo' protein folding / negative regulation of heart rate / negative regulation of phosphoprotein phosphatase activity / FK506 binding / positive regulation of axon regeneration / : / smooth muscle contraction / negative regulation of ryanodine-sensitive calcium-release channel activity / response to vitamin E / calcium channel inhibitor activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / protein peptidyl-prolyl isomerization / T cell proliferation / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / release of sequestered calcium ion into cytosol / regulation of ryanodine-sensitive calcium-release channel activity / Ion homeostasis / sarcoplasmic reticulum membrane / calcium channel complex / regulation of cytosolic calcium ion concentration / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / response to hydrogen peroxide / Stimuli-sensing channels / Z disc / positive regulation of cytosolic calcium ion concentration / protein refolding / transmembrane transporter binding / signaling receptor binding / membrane / cytosol / cytoplasm
Similarity search - Function
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
Similarity search - Domain/homology
Peptidyl-prolyl cis-trans isomerase FKBP1B
Similarity search - Component
Biological speciesSus scrofa (pig) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.0 Å
AuthorsWoll KW / Haji-Ghassemi O
Funding support1 items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR)
CitationJournal: Nat Commun / Year: 2021
Title: Pathological conformations of disease mutant Ryanodine Receptors revealed by cryo-EM.
Authors: Kellie A Woll / Omid Haji-Ghassemi / Filip Van Petegem /
Abstract: Ryanodine Receptors (RyRs) are massive channels that release Ca from the endoplasmic and sarcoplasmic reticulum. Hundreds of mutations are linked to malignant hyperthermia (MH), myopathies, and ...Ryanodine Receptors (RyRs) are massive channels that release Ca from the endoplasmic and sarcoplasmic reticulum. Hundreds of mutations are linked to malignant hyperthermia (MH), myopathies, and arrhythmias. Here, we explore the first MH mutation identified in humans by providing cryo-EM snapshots of the pig homolog, R615C, showing that it affects an interface between three solenoid regions. We also show the impact of apo-calmodulin (apoCaM) and how it can induce opening by bending of the bridging solenoid, mediated by its N-terminal lobe. For R615C RyR1, apoCaM binding abolishes a pathological 'intermediate' conformation, distributing the population to a mixture of open and closed channels, both different from the structure without apoCaM. Comparisons show that the mutation primarily affects the closed state, inducing partial movements linked to channel activation. This shows that disease mutations can cause distinct pathological conformations of the RyR and facilitate channel opening by disrupting interactions between different solenoid regions.
History
DepositionMar 4, 2020-
Header (metadata) releaseApr 1, 2020-
Map releaseJan 6, 2021-
UpdateMar 6, 2024-
Current statusMar 6, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.8
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.8
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6w1n
  • Surface level: 0.8
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_21513.png

Downloads & links

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Map

FileDownload / File: emd_21513.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFinal map from cryoSPARC
Voxel sizeX=Y=Z: 1.37083 Å
Density
Contour LevelBy AUTHOR: 0.8 / Movie #1: 0.8
Minimum - Maximum-1.5656805 - 3.4493966
Average (Standard dev.)-0.00042537882 (±0.12659301)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 658.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.37083333333331.37083333333331.3708333333333
M x/y/z480480480
origin x/y/z0.0000.0000.000
length x/y/z658.000658.000658.000
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ410410410
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS480480480
D min/max/mean-1.5663.449-0.000

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Supplemental data

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Additional map: Density modified map obtained from PHENIX Resolve

Fileemd_21513_additional_1.map
AnnotationDensity modified map obtained from PHENIX Resolve
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: composite map made from focused (masked) refinements conducted...

Fileemd_21513_additional_2.map
Annotationcomposite map made from focused (masked) refinements conducted in RELION
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_21513_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_21513_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : ryanodine receptor-FKBP1B complex

EntireName: ryanodine receptor-FKBP1B complex
Components
  • Complex: ryanodine receptor-FKBP1B complex
    • Complex: ryanodine receptor
      • Protein or peptide: Ryanodine Receptor
    • Complex: FKBP1B
      • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1B
  • Ligand: ZINC ION

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Supramolecule #1: ryanodine receptor-FKBP1B complex

SupramoleculeName: ryanodine receptor-FKBP1B complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2

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Supramolecule #2: ryanodine receptor

SupramoleculeName: ryanodine receptor / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: Sus scrofa (pig)

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Supramolecule #3: FKBP1B

SupramoleculeName: FKBP1B / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Peptidyl-prolyl cis-trans isomerase FKBP1B

MacromoleculeName: Peptidyl-prolyl cis-trans isomerase FKBP1B / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.939562 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SNAGVEIETI SPGDGRTFPK KGQTCVVHYT GMLQNGKKFD SSRDRNKPFK FRIGKQEVIK GFEEGAAQMS LGQRAKLTCT PDVAYGATG HPGVIPPNAT LIFDVELLNL E

UniProtKB: Peptidyl-prolyl cis-trans isomerase FKBP1B

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Macromolecule #2: Ryanodine Receptor

MacromoleculeName: Ryanodine Receptor / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 510.786406 KDa
SequenceString: MGDGGEGEDE VQFLRTDDEV VLQCNATVLK EQLKLCLAAE GFGNRLCFLE PTSNAQNVPP DLAICCFVLE QSLSVRALQE MLANTVEAG VESSQGGGHR TLLYGHAILL RHAHSGMYLS CLTTSRSMTD KLAFDVGLQE DATGEACWWT THPASKQRSE G EKVRVGDD ...String:
MGDGGEGEDE VQFLRTDDEV VLQCNATVLK EQLKLCLAAE GFGNRLCFLE PTSNAQNVPP DLAICCFVLE QSLSVRALQE MLANTVEAG VESSQGGGHR TLLYGHAILL RHAHSGMYLS CLTTSRSMTD KLAFDVGLQE DATGEACWWT THPASKQRSE G EKVRVGDD LILVSVSSER YLHLSTASGE LQVDASFMQT LWNMNPICSG CEEGYVTGGH VLRLFHGHMD ECLTISPADS DD QRRLVYY EGGSVCTHAR SLWRLEPLRI SWSGSHLRWG QPLRIRHVTT GRYLALIEDQ GLVVVDASKA HTKATSFCFR ISK EKLDTA PKRDVEGMGP PEIKYGESLC FVQHVASGLW LTYAAPDPKA LRLGVLKKKA ILHQEGHMDD ALSLTRCQQE ESQA ARMIY STAGLYNHFI KGLDSFSGKP RGSGAPAGTA LPLEGVILSL QDLIGYFEPP SEELQHEEKQ SKLRSLRNRQ SLFQE EGML SLVLNCIDRL NVYTTAAHFA EFAGEEAAES WKEIVNLLYE ILASLIRGNR ANCALFSNNL DWLVSKLDRL EASSGI LEV LYCVLIESPE VLNIIQENHI KSIISLLDKH GRNHKVLDVL CSLCVCNGVA VRSNQDLITE NLLPGRELLL QTNLINY VT SIRPNIFVGR AEGTTQYSKW YFEVMVDEVV PFLTAQATHL RVGWALTEGY SPYPGGGEGW GGNGVGDDLY SYGFDGLH L WTGHVPRLVT SPGQHLLAPE DVVSCCLDLS VPSISFRING CPVQGVFEAF NLNGLFFPVV SFSAGVKVRF LLGGRHGEF KFLPPPGYAP CHEAVLPRER LRLEPIKEYR REGPRGPHLV GPSRCLSHTD FVPCPVDTVQ IVLPPHLERI REKLAENIHE LWALTRIEQ GWTYGPVRDD NKRLHPCLVD FHSLPEPERN YNLQMSGETL KTLLALGCHV GMADEKAEDN LRKTKLPKTY M MSNGYKPA PLDLSHVRLT PAQTTLVDRL AENGHNVWAR DRVAQGWSYS AVQDIPARRN PRLVPYRLLD EATKRSNRDS LC QAVRTLL GYGYNIEPPD QEPSQVESQS RWDRVRIFRA EKSYAVQSGR WYFEFEAVTT GEMRVGWARP ELRPDVELGA DEL AYVFNG HRGQRWHLGS ELFGRPWQSG DVVGCMIDLT ENTIIFTLNG EVLMSDSGSE TAFRDIEVGD GFLPVCSLGP GQVG HLNLG QDVSSLRFFA ICGLQEGFEP FAINMQRPVT TWFSKSLPQF EAVPLEHPHY EVSRVDGTVD TPPCLRLTHR TWGSQ NSLV EMLFLRLSLP VQFHQHFRCT AGATPLAPPG LQPPAEDEAR AAEPDPDYEN LRRSAGRWGE AEGGKEGTAK EGAPGG TAQ AGVEAQPPRA ENEKDATTEK NKKRGFLFKA KKAAMMTQPP ATPTLPRLPH EVVPADDRDD PDIILNTTTY YYSVRVF AG QEPSCVWVGW VTPDYHQHDM NFDLTKVRAV TVTMGDEQGN IHSSLKCSNC YMVWGGDFVS PGQQGRISHT DLVIGCLV D LATGLMTFTA NGKESNTFFQ VEPNTKLFPA VFVLPTHQNV IQFELGKQKN IMPLSAAMFL SERKNPAPQC PPRLEMQML MPVSWSRMPN HFLRVETRRA GERLGWAVQC QEPLTMMALH IPEENRCMDI LELSERLDLQ QFHSHTLRLY RAVCALGNNR VAHALCSHV DQAQLLHALE DAHLPGPLRA GYYDLLISIH LESACRSRRS MLSEYIVPLT PETRAITLFP PGKRTENGPR R HGLPGVGV TTSLRPPHHF SAPCFVAALP AVGAAEAPAR LSPSIPLEAL RDKALRMLGE AVRDGGQHAR DPVGGSVEFQ FV PVLKLVS TLLVMGIFGD EDVKQILKMI EPEVFTEEEE EEEEEEEEEE EDEEEKEEDE EEEAREKEDE EKEEEETAEG EKE EYLEEG LLQMKLPESV KLQMCNLLEY FCDQELQHRV ESLAAFAERY VDKLQANQRD RYGILMKAFT MTAAETARRT REFR SPPQE QINMLLHFKD GEDEEDCPLP DEIRQDLLEF HQDLLTHCGI QLEGEEEEPE EEATLGSRLM SLLEKVRLVK KKEEK SEEE PPAEESKLQS LQELVSHTVV RWAQEDFVQS PELVRAMFSL LHRQYDGLGE LLRALPRAYT ISPSSVEDTM 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 EGGSGLLATI EEAIRISEDP ARDGPGVRR DRRREHFGEE PPEENRVHLG HAIMSFYAAL IDLLGRCAPE MHLIQAGKGE ALRIRAILRS LVPLDDLVGI ISLPLQIPTL GKDGALVQP KMSASFVPDH KASMVLFLDR VYGIENQDFL LHVLDVGFLP DMRAAASLDT ATFSTTEMAL ALNRYLCLAV L PLITKCAP LFAGTEHRAI MVDSMLHTVY RLSRGRSLTK AQRDVIEECL MALCRYIRPS MLQHLLRRLV FDVP(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)DPRPVET LNVIIPEK L DSFINKFAEY THEKWAFDKI QNNWSYGENI DEELKTHPML RPYKTFSEKD KEIYRWPIKE SLKAMIAWEW TIEKAREGE EEKTEKKKTR KISQSAQTYD AREGYNPQPP DLSGVTLSRE LQAMAEQLAE NYHNTWGRKK KQELEAKGGG THPLLVPYDT LTAKEKARD REKAQELLKF LQMNGYAVTR (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)PLLIRYV DNNRAHWLTE PNPSAEELFR MVGEIFIYWS K(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) SLRWQMALYR GLPGREEDA DDPEKIVRRV QEVSAVLYHL EQMEHPYKSK (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)MTPLYNLP THRACNM FL ESYKAAWILT EDHSFEDRMI DDLSKAGEQE EEEEEVEEKK PDPLHQLVLH FSRTALTEKS KLDEDYLYMA YADIMAKS C HLEEGGENGE AQEEVEVSFE EKEMEKQRLL YQQARLHNRG AAEMVLQMIS ACKGETGAMV SSTLKLGISI LNGGNADVQ QKMLDYLKDK KEVGFFQSIQ ALMQTCSVLD LNAFERQNKA EGLGMVNEDG TVINRQNGEK VMADDEFTQD LFRFLQLLCE GHNNDFQNY LRTQTGNTTT INIIICTVDY LLRLQESISD FYWYYSGKDV IEEQGKRNFS KAMSVAKQVF NSLTEYIQGP C TGNQQSLA HSRLWDAVVG FLHVFAHMMM KLAQDSSQIE LLKELLDLQK DMVVMLLSLL EGNVVNGMIA RQMVDMLVES SS NVEMILK FFDMFLKLKD IVGSEAFQDY VTDPRGLISK KDFQK(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)EEFANRFQ EPARDIGFNV AVLLTNLSEH VPHDPRLRNF LELAESILEY FRPYLGRIEI MGASRRIERI YFEISETNRA QWEMPQVKES KRQFIFDVV NEGGESEKME LFVSFCEDTI FEMQIAAQIS EPEGEPEEDE DEGAGLAEAG AEGAEEGAVG PEGAAGTAAA G LTARLAAA TSRALRGLSY RSLRRRVRRL RRLTAREAAT ALAALLWAAL AHAGAAGAGA AAGALRLLWG SLFGGGLVEG AK KVTVTEL LAGMPDPTGD EVHGEQPAGP GGEADGEGAG EGAGEAWEGA GDEEVAVQEA GPGGADGAVA VAEGGPFRPE GAG GLGDMG DTTPAEPPTP EGSPIIKRKL GVDGEEEELP PEPEPEPEPE PEKADAENGE KEEVPKPPPE PPKKTAPPPP PPKK EEGGS GGLEFWGELE VQRVKFLNYL SRNFYTLRFL ALFLAFAINF ILLFYKVSDS PPGEDDMEGS AAGDLSGAGS GGGSG WGSG AGEEVEGDED ENMVYYFLEE STGYMEPALR CLSLLHTLVA FLCIIGYNCL KVPLVIFKRE KELARKLEFD GLYITE QPE DDDVKGQWDR LVLNTPSFPS NYWDKFVKRK VLDKHGDIYG RERIAELLGM DLATLEITAH NERKPEPPPG LLTWLMS ID VKYQIWKFGV IFTDNSFLYL GWYMVMSLLG HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYL Y TVVAFNFFRK FYNKSEDEDE PDMKCDDMMT CYLFHMYVGV RAGGGIGDEI EDPAGDEYEL YRVVFDITFF FFVIVILLA IIQGLIIDAF GELRDQQEQV REDMETKCFI CGIGSDYFDT TPHRFETHTL EEHNLANYMF FLMYLINKDE TEHTGQESYV WKMYQERCW DFFPAGDCFR KQYEDQLS

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Macromolecule #3: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 3 / Number of copies: 4 / Formula: ZN
Molecular weightTheoretical: 65.409 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: 7.5
GridMaterial: GRAPHENE OXIDE
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: OTHER / Imaging mode: DIFFRACTION
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 30.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionApplied symmetry - Point group: C4 (4 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 4.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: PHENIX (ver. dev-3714) / Number images used: 52289

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