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- EMDB-22019: Pig R615C RyR1 in complex with CaM, EGTA (class 3, closed) -

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Basic information

Entry
Database: EMDB / ID: EMD-22019
TitlePig R615C RyR1 in complex with CaM, EGTA (class 3, closed)
Map dataRELION postprocessed map
Sample
  • Complex: ryanodine receptor-FKBP1B-calmodulin complex
    • Complex: ryanodine receptor
      • Protein or peptide: Ryanodine Receptor
    • Complex: FKBP1B
      • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1B
    • Complex: Calmodulin
      • Protein or peptide: Calmodulin-1
Keywordsreceptor / calcium / channel / complex / TRANSPORT PROTEIN-ISOMERASE-CALCIUM BINDING PROTEIN complex
Function / homology
Function and homology information


positive regulation of sequestering of calcium ion / negative regulation of calcium-mediated signaling / negative regulation of insulin secretion involved in cellular response to glucose stimulus / neuronal action potential propagation / negative regulation of release of sequestered calcium ion into cytosol / insulin secretion involved in cellular response to glucose stimulus / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events ...positive regulation of sequestering of calcium ion / negative regulation of calcium-mediated signaling / negative regulation of insulin secretion involved in cellular response to glucose stimulus / neuronal action potential propagation / negative regulation of release of sequestered calcium ion into cytosol / insulin secretion involved in cellular response to glucose stimulus / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / response to redox state / positive regulation of ryanodine-sensitive calcium-release channel activity / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Loss of phosphorylation of MECP2 at T308 / 'de novo' protein folding / CREB1 phosphorylation through the activation of Adenylate Cyclase / CaMK IV-mediated phosphorylation of CREB / PKA activation / negative regulation of high voltage-gated calcium channel activity / negative regulation of heart rate / Glycogen breakdown (glycogenolysis) / CLEC7A (Dectin-1) induces NFAT activation / Activation of RAC1 downstream of NMDARs / organelle localization by membrane tethering / negative regulation of ryanodine-sensitive calcium-release channel activity / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / FK506 binding / negative regulation of calcium ion export across plasma membrane / regulation of cardiac muscle cell action potential / presynaptic endocytosis / Synthesis of IP3 and IP4 in the cytosol / regulation of cell communication by electrical coupling involved in cardiac conduction / Phase 0 - rapid depolarisation / calcineurin-mediated signaling / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / RHO GTPases activate PAKs / Ion transport by P-type ATPases / Uptake and function of anthrax toxins / regulation of ryanodine-sensitive calcium-release channel activity / Long-term potentiation / protein phosphatase activator activity / Calcineurin activates NFAT / Regulation of MECP2 expression and activity / smooth muscle contraction / DARPP-32 events / catalytic complex / Smooth Muscle Contraction / detection of calcium ion / regulation of cardiac muscle contraction / RHO GTPases activate IQGAPs / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / T cell proliferation / calcium channel inhibitor activity / cellular response to interferon-beta / Protein methylation / presynaptic cytosol / Activation of AMPK downstream of NMDARs / Ion homeostasis / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / eNOS activation / titin binding / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / sperm midpiece / voltage-gated potassium channel complex / regulation of calcium-mediated signaling / release of sequestered calcium ion into cytosol / calcium channel complex / substantia nigra development / FCERI mediated Ca+2 mobilization / sarcoplasmic reticulum membrane / calcium channel regulator activity / Ras activation upon Ca2+ influx through NMDA receptor / regulation of heart rate / FCGR3A-mediated IL10 synthesis / calyx of Held / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / protein maturation / adenylate cyclase activator activity / sarcomere / VEGFR2 mediated cell proliferation / regulation of cytokinesis / protein serine/threonine kinase activator activity / VEGFR2 mediated vascular permeability / spindle microtubule / peptidyl-prolyl cis-trans isomerase activity / Translocation of SLC2A4 (GLUT4) to the plasma membrane / peptidylprolyl isomerase / positive regulation of receptor signaling pathway via JAK-STAT / RAF activation / calcium-mediated signaling / Transcriptional activation of mitochondrial biogenesis / cellular response to type II interferon / Stimuli-sensing channels / long-term synaptic potentiation / Z disc / response to calcium ion
Similarity search - Function
: / FKBP-type peptidyl-prolyl cis-trans isomerase / FKBP-type peptidyl-prolyl cis-trans isomerase domain / FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / Peptidyl-prolyl cis-trans isomerase domain superfamily / : / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. ...: / FKBP-type peptidyl-prolyl cis-trans isomerase / FKBP-type peptidyl-prolyl cis-trans isomerase domain / FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / Peptidyl-prolyl cis-trans isomerase domain superfamily / : / EF-hand domain pair / 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 / EF-hand domain pair
Similarity search - Domain/homology
Calmodulin-1 / Peptidyl-prolyl cis-trans isomerase FKBP1B
Similarity search - Component
Biological speciesSus scrofa (pig) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.7 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
DepositionMay 21, 2020-
Header (metadata) releaseJan 13, 2021-
Map releaseJan 13, 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: 0.00027
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.00027
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6x36
  • Surface level: 0.00027
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_22019.png

Downloads & links

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Map

FileDownload / File: emd_22019.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationRELION postprocessed map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 480 pix.
= 523.2 Å		1.09 Å/pix.
x 480 pix.
= 523.2 Å		1.09 Å/pix.
x 480 pix.
= 523.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.09 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.00027 / Movie #1: 0.00027
Minimum - Maximum-0.0006940387 - 0.0016943889
Average (Standard dev.)0.000003986756 (±0.000042950112)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 523.2 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.091.091.09
M x/y/z480480480
origin x/y/z0.0000.0000.000
length x/y/z523.200523.200523.200
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-0.0010.0020.000

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Supplemental data

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Additional map: Density modified map generated from RELION half maps...

Fileemd_22019_additional_1.map
AnnotationDensity modified map generated from RELION half maps using PHENIX Resolve
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_22019_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_22019_half_map_2.map
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Sample components

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Entire : ryanodine receptor-FKBP1B-calmodulin complex

EntireName: ryanodine receptor-FKBP1B-calmodulin complex
Components
  • Complex: ryanodine receptor-FKBP1B-calmodulin complex
    • Complex: ryanodine receptor
      • Protein or peptide: Ryanodine Receptor
    • Complex: FKBP1B
      • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1B
    • Complex: Calmodulin
      • Protein or peptide: Calmodulin-1

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Supramolecule #1: ryanodine receptor-FKBP1B-calmodulin complex

SupramoleculeName: ryanodine receptor-FKBP1B-calmodulin complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all

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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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Supramolecule #4: Calmodulin

SupramoleculeName: Calmodulin / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #3
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: 392.424781 KDa
SequenceString: QFLRTDDEVV LQCNATVLKE QLKLCLAAEG FGNRLCFLEP TSNAQNVPPD LAICCFVLEQ SLSVRALQEM LANGHRTLLY GHAILLRHA HSGMYLSCLT TSRSMTDKLA FDVGLQEDAT GEACWWTTHP ASKQRSEGEK VRVGDDLILV SVSSERYLHL S TASGELQV ...String:
QFLRTDDEVV LQCNATVLKE QLKLCLAAEG FGNRLCFLEP TSNAQNVPPD LAICCFVLEQ SLSVRALQEM LANGHRTLLY GHAILLRHA HSGMYLSCLT TSRSMTDKLA FDVGLQEDAT GEACWWTTHP ASKQRSEGEK VRVGDDLILV SVSSERYLHL S TASGELQV DASFMQTLWN MNPICSGCEE GYVTGGHVLR LFHGHMDECL TISPADQRRL VYYEGGSVCT HARSLWRLEP LR ISWSGSH LRWGQPLRIR HVTTGRYLAL IEDQGLVVVD ASKAHTKATS FCFRISKEKL KRDVEGMGPP EIKYGESLCF VQH VASGLW LTYAALKKKA ILHQEGHMDD ALSLTRCQQE ESQAARMIYS TAGLYNHFIK GLDSFSGKPR PAGTALPLEG VILS LQDLI GYFEPPSEEL QHEEKQSKLR SLRNRQSLFQ EEGMLSLVLN CIDRLNVYTT AAHFAEFAGE EAAESWKEIV NLLYE ILAS LIRGNRANCA LFSNNLDWLV SKLDRLEASS GILEVLYCVL IESPEVLNII QENHIKSIIS LLDKHGRNHK VLDVLC SLC VCNGVAVCSN QDLITENLLP GRELLLQTNL INYVTSIRPN IFVGRAEGTT QYSKWYFEVM VDEVVPFLTA QATHLRV GW ALTEGYSPYP GGGEGWGGNG VGDDLYSYGF DGLHLWTGHV PRLVTSPGQH LLAPEDVVSC CLDLSVPSIS FRINGCPV Q GVFEAFNLNG LFFPVVSFSA GVKVRFLLGG RHGEFKFLPP PGYAPCHEAV LPRERLRLEP IKEYRREGPR PHLVGPSRC LSHTDFVPCP IREKLAENIH ELWALTRIEQ GWTYGPVRHP CLVDFHSLPE PERNYNLQMS GETLKTLLAL GCHVGMADEK AEDNLRKTK LPKTYMMSNG YKPAPLDLSH VRLTPAQTTL VDRLAENGHN VWARDRVAQG WSYSAVQDIP ARRNPRLVPY R LLDEATKR SNRDSLCQAV RTLLGYGRVR IFRAEKSYAV QSGRWYFEFE AVTTGEMRVG WARPELRPDV ELGADELAYV FN GHRGQRW HLGSELFGRP WQSGDVVGCM IDLTENTIIF TLNGEVLMSD SGSETAFRDI EVGDGFLPVC SLGPGQVGHL NLG QDVSSL RFFAICGLQE GFEPFAINMQ RPVTTWFSKS LPQFEAVPLE HPHYEVSRVD GTVDTPPCLR LTHRQNSLVE MLFL RLSLP VQFHQLNTTT YYYSVRVFAG QEPSCVWVGW VTPDYHQHDM NFDLTKVRAV TVTMGDNIHS SLKCSNCYMV WGGDF VSHT DLVIGCLVDL ATGLMTFTAN GKESNTFFQV EPNTKLFPAV FVLPTHQNVI QFELGKNIMP LSAAMFLSER KNPAPQ CPP RLEMQMLMPV SWSRMPNHFL RVETRRAGER LGWAVQCQEP LTMMALHIPE ENRCMDILEL SERLDLQQFH SHTLRLY RA VCALGNNRVA HALCSHVDQA QLLHALEDAH LPGPLRAGYY DLLISIHLES ACRSRRSMLS EYIVPLTPET RAITLFPP R HGLPGVGVTT SLRPPHHFSA PCFVAALPEA PARLSPSIPL EALRDKALRM LGEAVRDGGQ HARDPVGGSV EFQFVPVLK LVSTLLVMGI FGDEDVKQIL KMIEPEVEEG LLQMKLPESV KLQMCNLLEY FCDQELQHRV ESLAAFAERY VDKLQANQRD RYGILMKAF TMTAAETARR TREFRSPPQE QINMLLHFKD CPLPDEIRQD LLEFHQDLLT HCGIQLQSLQ ELVSHTVVRW A QEDFVQSP ELVRAMFSLL HRQYDGLGEL LRALPRAYTI SPSSVEDTMS LLECLGQIRS LLIVQMGPQE ENLMIQSIGN IM NNKVFYQ HPNLMRALGM HETVMEVMVN VLGRFPKMVT SCCRFLCYFC RISRQNQRSM FDHLSYLLEN SGGMQGSTPL DVA AASVID NNELALALQE QDLEKVVSYL AGCGLQSCPM LLAKGYPDIG WNPCGGERYL DFLRFAVFVN GESVEENANV VVRL LIRKP ECFGPLLATI EEAMSFYAAL IDLLGRCAPI QAGKGEALRI RAILRSLVPL DDLVGIISLP LQIPTPDHKA SMVLF LDRA LALNRYLCLA VLPLITKCAP LMVDSMLHTV YRLSRGRSLT KAQRDVIEEC LMALCRYIPS MLQHLLRRLV F(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)(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)EFSVL C RDLYALYPLL IRYVDNNRAH WLPSAEELFR MVGEIFIYWS KSHNFKREEQ NFVV(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)RRAVVAC FRMTPLYNLP THR ACNMFL ESYKAAWILT EDHSFEDRMI DDLSKAGEKK PDPLHQLVLH FSRTALTEKS KLDEDYLYMA YADIMAKSCH LEES FEEKE MEKQRLLYQQ ARLHNRGAAE MVLQMISACK GETGAMVSST LKLGISILNG GNADVQQKML DYLKDKKEVG FFQSI QALM QTCSVLDLNA FERQNKAEGL GMVNEDGTVI NRQNGEKVMA DDEFTQDLFR FLQLLCEGHN NDFQNYLRTQ TGNTTT INI IICTVDYLLR LQESISDFYW YYSGKDVIEE QGKRNFSKAM SVAKQVFNSL TEYIQGPCTG NQQSLAHSRL WDAVVGF LH VFAHMMMKLA LKELLDLQKD MVVMLLSLLE GNVVNGMIAR QMVDMLVESS SNVEMILKFF DMFLKLKDIV GSEAFQDY V TDPRGLISKK DFQK(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) EFANRFQEPA RDIGFNVAVL LTNLSEHVPH DPRLR NFLE LAESILEYFR PYLGRIEIMG ASRRIERIYF EISETNRAQW EMPQVKESKR QFIFDVVNGE SEKMELFVSF CEDTIF EMQ (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)EV QRVKFLNYLS RNFYTLRFLA LFLAFAINFI LLFYKVSDSP PVYYFLEEST GYMEPALRCL SLLHTLVA F LCIIGYNCLK VPLVIFKREK ELARKLEFDG LYITEQPEDD DVKGQWDRLV LNTPSFPSNY WDKFVKRKVL DKHGDIYGR ERIAELTWLM SIDVKYQIWK FGVIFTDNSF LYLGWYMVMS LLGHYNNFFF AAHLLDIAMG VKTLRTILSS VTHNGKQLVM TVGLLAVVV YLYTVVAFNF FRKFYNKSKC DDMMTCYLFH MYVGVRAGGG IGDEIEDPAG DEYELYRVVF DITFFFFVIV I LLAIIQGL IIDAFGELRD QQEQVREDME TKCFICGIGS DYFDTTPHRF ETHTLEEHNL ANYMFFLMYL INKDETEHTG QE SYVWKMY QERCWDFFPA GDCFRKQYED QL

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Macromolecule #3: Calmodulin-1

MacromoleculeName: Calmodulin-1 / type: protein_or_peptide / ID: 3 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.723365 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREA FRVFDKDGNG YISAAELRHV MTNLGEKLTD EEVDEMIREA DIDGDGQVNY EEFVQMMTA

UniProtKB: Calmodulin-1

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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
GridDetails: unspecified
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: DIFFRACTION
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
Final reconstructionApplied symmetry - Point group: C4 (4 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 4.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: PHENIX (ver. dev-3714) / Number images used: 7038
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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