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- EMDB-22018: Pig R615C RyR1 in complex with CaM, EGTA (class 1, open) -

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Open data


ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-22018
TitlePig R615C RyR1 in complex with CaM, EGTA (class 1, open)
Map dataRyR1, FKBP12.6, CaM
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
  • Ligand: ZINC ION
Keywordsreceptor / calcium / channel / complex / TRANSPORT PROTEIN-ISOMERASE-CALCIUM BINDING PROTEIN complex
Function / homology
Function and homology information


positive regulation of sequestering of calcium ion / cyclic nucleotide binding / negative regulation of calcium-mediated signaling / negative regulation of insulin secretion involved in cellular response to glucose stimulus / negative regulation of release of sequestered calcium ion into cytosol / neuronal action potential propagation / insulin secretion involved in cellular response to glucose stimulus / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers ...positive regulation of sequestering of calcium ion / cyclic nucleotide binding / negative regulation of calcium-mediated signaling / negative regulation of insulin secretion involved in cellular response to glucose stimulus / negative regulation of release of sequestered calcium ion into cytosol / neuronal action potential propagation / insulin secretion involved in cellular response to glucose stimulus / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / Reduction of cytosolic Ca++ levels / response to redox state / Activation of Ca-permeable Kainate Receptor / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / 'de novo' protein folding / PKA activation / CaMK IV-mediated phosphorylation of CREB / 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 / negative regulation of calcium ion export across plasma membrane / organelle localization by membrane tethering / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / FK506 binding / presynaptic endocytosis / regulation of cardiac muscle cell action potential / positive regulation of axon regeneration / positive regulation of ryanodine-sensitive calcium-release channel activity / Synthesis of IP3 and IP4 in the cytosol / regulation of cell communication by electrical coupling involved in cardiac conduction / Phase 0 - rapid depolarisation / Negative regulation of NMDA receptor-mediated neuronal transmission / negative regulation of ryanodine-sensitive calcium-release channel activity / Unblocking of NMDA receptors, glutamate binding and activation / RHO GTPases activate PAKs / calcineurin-mediated signaling / Ion transport by P-type ATPases / Uptake and function of anthrax toxins / Long-term potentiation / Regulation of MECP2 expression and activity / Calcineurin activates NFAT / protein phosphatase activator activity / regulation of ryanodine-sensitive calcium-release channel activity / DARPP-32 events / smooth muscle contraction / response to vitamin E / Smooth Muscle Contraction / catalytic complex / 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 / presynaptic cytosol / calcium channel inhibitor activity / cellular response to interferon-beta / Protein methylation / Activation of AMPK downstream of NMDARs / T cell proliferation / Ion homeostasis / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / eNOS activation / regulation of calcium-mediated signaling / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / titin binding / voltage-gated potassium channel complex / sarcoplasmic reticulum membrane / release of sequestered calcium ion into cytosol / calcium channel regulator activity / sperm midpiece / substantia nigra development / calcium channel complex / calyx of Held / FCERI mediated Ca+2 mobilization / Ras activation upon Ca2+ influx through NMDA receptor / protein maturation / FCGR3A-mediated IL10 synthesis / adenylate cyclase activator activity / regulation of heart rate / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / protein serine/threonine kinase activator activity / VEGFR2 mediated cell proliferation / peptidyl-prolyl cis-trans isomerase activity / sarcomere / regulation of cytokinesis / VEGFR2 mediated vascular permeability / RNA polymerase II CTD heptapeptide repeat P3 isomerase activity / RNA polymerase II CTD heptapeptide repeat P6 isomerase activity / Translocation of SLC2A4 (GLUT4) to the plasma membrane / positive regulation of receptor signaling pathway via JAK-STAT / spindle microtubule / peptidylprolyl isomerase / RAF activation / calcium-mediated signaling / Transcriptional activation of mitochondrial biogenesis
Similarity search - Function
: / FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / FKBP-type peptidyl-prolyl cis-trans isomerase / FKBP-type peptidyl-prolyl cis-trans isomerase domain / 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 domain profile. / FKBP-type peptidyl-prolyl cis-trans isomerase / FKBP-type peptidyl-prolyl cis-trans isomerase domain / 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: 4.2 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: 0.023
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.023
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6x35
  • Surface level: 0.023
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_22018.png

Downloads & links

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Map

FileDownload / File: emd_22018.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationRyR1, FKBP12.6, CaM
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)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.09 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.023 / Movie #1: 0.023
Minimum - Maximum-0.14669418 - 0.19171208
Average (Standard dev.)-0.000000000037294 (±0.0044705574)
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-0.1470.192-0.000

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Supplemental data

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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
  • Ligand: ZINC ION

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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: #1-#3

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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: 423.654469 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 GPHLVGPSR CLSHTDFVPC PLPPHLERIR EKLAENIHEL WALTRIEQGW TYGPVRDDNK RLHPCLVDFH SLPEPERNYN LQMSGETLKT LLALGCHVG MADEKAEDNL RKTKLPKTYM MSNGYKPAPL DLSHVRLTPA QTTLVDRLAE NGHNVWARDR VAQGWSYSAV Q DIPARRNP RLVPYRLLDE ATKRSNRDSL CQAVRTLLGY GRVRIFRAEK SYAVQSGRWY FEFEAVTTGE MRVGWARPEL RP DVELGAD ELAYVFNGHR GQRWHLGSEL FGRPWQSGDV VGCMIDLTEN TIIFTLNGEV LMSDSGSETA FRDIEVGDGF LPV CSLGPG QVGHLNLGQD VSSLRFFAIC GLQEGFEPFA INMQRPVTTW FSKSLPQFEA VPLEHPHYEV SRVDGTVDTP PCLR LTHRS LVEMLFLRLS LPVQFHQLNT TTYYYSVRVF AGQEPSCVWV GWVTPDYHQH DMNFDLTKVR AVTVTMGDNI HSSLK CSNC YMVWGGDFVS HTDLVIGCLV DLATGLMTFT ANGKESNTFF QVEPNTKLFP AVFVLPTHQN VIQFELGKQK NIMPLS AAM FLSERKNPAP QCPPRLEMQM LMPVSWSRMP NHFLRVETRR AGERLGWAVQ CQEPLTMMAL HIPEENRCMD ILELSER LD LQQFHSHTLR LYRAVCALGN NRVAHALCSH VDQAQLLHAL EDAHLPGPLR AGYYDLLISI HLESACRSRR SMLSEYIV P LTPETRAITL FPPRHGLPGV GVTTSLRPPH HFSAPCFVAA LPEAPARLSP SIPLEALRDK ALRMLGEAVR DGGQHARDP VGGSVEFQFV PVLKLVSTLL VMGIFGDEDV KQILKMIEPE VEEGLLQMKL PESVKLQMCN LLEYFCDQEL QHRVESLAAF AERYVDKLQ ANQRDRYGIL MKAFTMTAAE TARRTREFRS PPQEQINMLL HFKPLPDEIR QDLLEFHQDL LTHCGIQLQS L QELVSHTV VRWAQEDFVQ SPELVRAMFS LLHRQYDGLG ELLRALPRAY TISPSSVEDT MSLLECLGQI RSLLIVQMGP QE ENLMIQS IGNIMNNKVF YQHPNLMRAL GMHETVMEVM VNVLGRFPKM VTSCCRFLCY FCRISRQNQR SMFDHLSYLL ENS GSTPLD VAAASVIDNN ELALALQEQD LEKVVSYLAG CGLQSCPMLL AKGYPDIGWN PCGGERYLDF LRFAVFVNGE SVEE NANVV VRLLIRKPEC FGPALRLLAT IEEAIGHAIM SFYAALIDLL GRCAPEMHLI QAGKGEALRI RAILRSLVPL DDLVG IISL PLQIPLMSAS FVPDHKASMV LFLDRVYGIE FLLHVLDVGF EMALALNRYL CLAVLPLITK CAPLFAMVDS MLHTVY RLS RGRSLTKAQR DVIEECLMAL CRYIRPSMLQ HLLRRLVF(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)DPR PVETLNVIIP EKLDSFINKF AEYTHEKWAF DKIQNNWSYG EN IDEELKT HPMLRPYKTF SEKDKEIYRW PIKESLKAMI AWEWTIEKAR EGEYNPQPPD LSGVTLSREL QAMAEQLAEN YHN TWGRKK KQELEAKGGG THPLLVPYDT LTAKEKARDR EKAQELLKFL QMNGYAVTR(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)EFSVLCR DLYALYPLLI RYVDNNRAHW LTEPNPSAEE LFRMVGEI F IYWSKSHNFK REEQNFVV(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) RRAVVACFRM TPLYNLPTHR ACNMFLESYK AAWILTEDHS FEDRMIDDL SKAGEQEEEE EEVEEKKPDP LHQLVLHFSR TALTEKSKLD EDYLYMAYAD IMAKSCHLEE SFEEKEMEKQ R LLYQQARL HNRGAAEMVL QMISACKGET GAMVSSTLKL GISILNGGNA DVQQKMLDYL KDKKEVGFFQ SIQALMQTCS VL DLNAFER QNKAEGLGMV NEDGTVIGEK VMADDEFTQD LFRFLQLLCE GHNNDFQNYL RTQTGNTTTI NIIICTVDYL LRL QESISD FYWYYSGKDV IEEQGKRNFS KAMSVAKQVF NSLTEYIQGP CTGNQQSLAH SRLWDAVVGF LHVFAHMMMK LAQD SSQIE LLKELLDLQK DMVVMLLSLL EGNVVNGMIA RQMVDMLVES SSNVEMILKF FDMFLKLKDI VGSEAFQDYV TDPRG LISK KDFQK(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)EEFANRFQE PARDIGFNVA VLLTNLSEHV PHDPRLRNFL EL AESILEY FRPYLGRIEI MGASRRIERI YFEISETNRA QWEMPQVKES KRQFIFDVVN EGGESEKMEL FVSFCEDTIF EMQ (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)EVQRVKFL NYLSRNFYTL RFLALFLAFA INFILLFYKV SDSPPVYYFL EESTGYMEPA LRCLSLLHTL VAFLCII GY NCLKVPLVIF KREKELARKL EFDGLYITEQ PEDDDVKGQW DRLVLNTPSF PSNYWDKFVK RKVLDKHGDI YGRERIAE G LLTWLMSIDV KYQIWKFGVI FTDNSFLYLG WYMVMSLLGH YNNFFFAAHL LDIAMGVKTL RTILSSVTHN GKQLVMTVG LLAVVVYLYT VVAFNFFRKF YNKSEDEDEP DMKCDDMMTC YLFHMYVGVR AGGGIGDEIE DPAGDEYELY RVVFDITFFF FVIVILLAI IQGLIIDAFG ELRDQQEQVR EDMETKCFIC GIGSDYFDTT PHRFETHTLE EHNLANYMFF LMYLINKDET E HTGQESYV WKMYQERCWD FFPAGDCFRK QYEDQL

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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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Macromolecule #4: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 4 / 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
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 reconstructionResolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: PHENIX (ver. dev-3714) / Number images used: 25122
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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