[English] 日本語
Yorodumi
- EMDB-26943: Consensus refinement of human erythrocyte ankyrin-1 complex (Comp... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-26943
TitleConsensus refinement of human erythrocyte ankyrin-1 complex (Composite map)
Map dataCombined map (composite of EMD-26916, EMD-26917, EMD-26918, EMD-26919, EMD-26940, aligned to global reconstruction). Maps are resampled on a 2x finer grid to facilitate visualization.
Sample
  • Complex: Band 3 anion exchanger complexed with glycophorin A, in outward facing state
    • Protein or peptide: x 6 types
  • Ligand: x 6 types
KeywordsMembrane Protein / Anion Exchange / Erythrocyte / Glycoprotein / TRANSPORT PROTEIN-STRUCTURAL PROTEIN complex
Function / homology
Function and homology information


methylammonium transmembrane transport / Defective RHAG causes regulator type Rh-null hemolytic anemia (RHN) / Rhesus blood group biosynthesis / methylammonium transmembrane transporter activity / Rhesus glycoproteins mediate ammonium transport / carbon dioxide transmembrane transport / carbon dioxide transmembrane transporter activity / ammonium homeostasis / spectrin-associated cytoskeleton / hemoglobin metabolic process ...methylammonium transmembrane transport / Defective RHAG causes regulator type Rh-null hemolytic anemia (RHN) / Rhesus blood group biosynthesis / methylammonium transmembrane transporter activity / Rhesus glycoproteins mediate ammonium transport / carbon dioxide transmembrane transport / carbon dioxide transmembrane transporter activity / ammonium homeostasis / spectrin-associated cytoskeleton / hemoglobin metabolic process / positive regulation of organelle organization / protein-glutamine gamma-glutamyltransferase activity / leak channel activity / maintenance of epithelial cell apical/basal polarity / pH elevation / Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tubular acidosis (dRTA) and dRTA with hemolytic anemia (dRTA-HA) / negative regulation of urine volume / NrCAM interactions / Neurofascin interactions / ammonium transmembrane transport / Bicarbonate transporters / intracellular monoatomic ion homeostasis / ammonium channel activity / ankyrin-1 complex / CHL1 interactions / plasma membrane phospholipid scrambling / monoatomic anion transmembrane transporter activity / cytoskeletal anchor activity / chloride:bicarbonate antiporter activity / solute:inorganic anion antiporter activity / bicarbonate transport / bicarbonate transmembrane transporter activity / M band / monoatomic anion transport / inorganic cation transmembrane transport / Interaction between L1 and Ankyrins / chloride transport / chloride transmembrane transporter activity / ankyrin binding / negative regulation of glycolytic process through fructose-6-phosphate / hemoglobin binding / spectrin binding / cortical cytoskeleton / erythrocyte maturation / exocytosis / axolemma / endoplasmic reticulum to Golgi vesicle-mediated transport / erythrocyte development / COPI-mediated anterograde transport / spleen development / protein-membrane adaptor activity / chloride transmembrane transport / cytoskeleton organization / sarcoplasmic reticulum / protein localization to plasma membrane / regulation of intracellular pH / Cell surface interactions at the vascular wall / carbon dioxide transport / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / cell morphogenesis / transmembrane transport / sarcolemma / structural constituent of cytoskeleton / Z disc / multicellular organismal-level iron ion homeostasis / cytoplasmic side of plasma membrane / blood coagulation / virus receptor activity / regulation of cell shape / ATPase binding / basolateral plasma membrane / protein phosphatase binding / postsynaptic membrane / blood microparticle / transmembrane transporter binding / cytoskeleton / neuron projection / structural molecule activity / enzyme binding / signal transduction / protein homodimerization activity / extracellular exosome / nucleoplasm / ATP binding / identical protein binding / membrane / plasma membrane / cytosol
Similarity search - Function
Blood group Rhesus C/E/D polypeptide / Glycophorin, conserved site / : / Glycophorin A / Glycophorin A signature. / Glycophorin / Ankyrin, UPA domain / UPA domain / Ammonium transporter AmtB-like domain / Ammonium Transporter Family ...Blood group Rhesus C/E/D polypeptide / Glycophorin, conserved site / : / Glycophorin A / Glycophorin A signature. / Glycophorin / Ankyrin, UPA domain / UPA domain / Ammonium transporter AmtB-like domain / Ammonium Transporter Family / Transglutaminase, N-terminal / Transglutaminase, C-terminal / Transglutaminase, active site / Protein-glutamine gamma-glutamyltransferase, animal / Transglutaminase, C-terminal domain superfamily / : / Transglutaminase family / Transglutaminase family, C-terminal ig like domain / Transglutaminases active site. / Ammonium/urea transporter / Domain present in ZO-1 and Unc5-like netrin receptors / ZU5 domain / ZU5 domain / ZU5 domain profile. / Transglutaminase-like superfamily / Transglutaminase/protease-like homologues / Transglutaminase-like / Anion exchange protein 1 / Transglutaminase-like superfamily / Anion exchange protein / Anion exchange, conserved site / Anion exchangers family signature 1. / Anion exchangers family signature 2. / Band 3 cytoplasmic domain / Band 3 cytoplasmic domain / Phosphotransferase/anion transporter / Bicarbonate transporter, eukaryotic / Bicarbonate transporter-like, transmembrane domain / HCO3- transporter integral membrane domain / Ankyrin repeat / Death domain profile. / DEATH domain, found in proteins involved in cell death (apoptosis). / Death domain / Death domain / Death-like domain superfamily / Ankyrin repeat / Papain-like cysteine peptidase superfamily / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Immunoglobulin E-set / Immunoglobulin-like fold
Similarity search - Domain/homology
Glycophorin-A / Band 3 anion transport protein / Ankyrin-1 / Protein 4.2 / Blood group Rh(CE) polypeptide / Ammonium transporter Rh type A
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.4 Å
AuthorsVallese F / Kim K / Yen LY / Johnston JD / Noble AJ / Cali T / Clarke OB
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nat Struct Mol Biol / Year: 2022
Title: Architecture of the human erythrocyte ankyrin-1 complex.
Authors: Francesca Vallese / Kookjoo Kim / Laura Y Yen / Jake D Johnston / Alex J Noble / Tito Calì / Oliver Biggs Clarke /
Abstract: The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association ...The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.2, glycophorin A and glycophorin B. The distinct T-shaped conformation of membrane-bound ankyrin-1 facilitates recognition of RhCE and, unexpectedly, the water channel aquaporin-1. Together, our results uncover the molecular details of ankyrin-1 association with the erythrocyte membrane, and illustrate the mechanism of ankyrin-mediated membrane protein clustering.
History
DepositionMay 10, 2022-
Header (metadata) releaseJul 20, 2022-
Map releaseJul 20, 2022-
UpdateOct 16, 2024-
Current statusOct 16, 2024Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

emd_26943.png

Downloads & links

-
Map

FileDownload / File: emd_26943.map.gz / Format: CCP4 / Size: 2.7 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCombined map (composite of EMD-26916, EMD-26917, EMD-26918, EMD-26919, EMD-26940, aligned to global reconstruction). Maps are resampled on a 2x finer grid to facilitate visualization.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.42 Å/pix.
x 900 pix.
= 373.5 Å		0.42 Å/pix.
x 900 pix.
= 373.5 Å		0.42 Å/pix.
x 900 pix.
= 373.5 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.415 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.2
Minimum - Maximum-0.11903254 - 6.6875954
Average (Standard dev.)0.006361343 (±0.08536767)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions900900900
Spacing900900900
CellA=B=C: 373.5 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Additional map: Combined map (composite of EMD-26916, EMD-26917, EMD-26918, EMD-26919,...

Fileemd_26943_additional_1.map
AnnotationCombined map (composite of EMD-26916, EMD-26917, EMD-26918, EMD-26919, EMD-26940, aligned to global reconstruction).
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Additional map: Mask used for FSC calculation of consensus refinement.

Fileemd_26943_additional_2.map
AnnotationMask used for FSC calculation of consensus refinement.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Additional map: Combined map (composite of EMD-26916, EMD-26917, EMD-26918, EMD-26919,...

Fileemd_26943_additional_3.map
AnnotationCombined map (composite of EMD-26916, EMD-26917, EMD-26918, EMD-26919, EMD-26940, aligned to global reconstruction). Unsharpened.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Additional map: Consensus refinement (unfiltered half map 1)

Fileemd_26943_additional_4.map
AnnotationConsensus refinement (unfiltered half map 1)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Additional map: Consensus refinement (unfiltered half map 2)

Fileemd_26943_additional_5.map
AnnotationConsensus refinement (unfiltered half map 2)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Additional map: Consensus refinement (unsharpened)

Fileemd_26943_additional_6.map
AnnotationConsensus refinement (unsharpened)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Additional map: Consensus refinement (sharpened)

Fileemd_26943_additional_7.map
AnnotationConsensus refinement (sharpened)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

+
Entire : Band 3 anion exchanger complexed with glycophorin A, in outward f...

EntireName: Band 3 anion exchanger complexed with glycophorin A, in outward facing state
Components
  • Complex: Band 3 anion exchanger complexed with glycophorin A, in outward facing state
    • Protein or peptide: Blood group Rh(CE) polypeptide
    • Protein or peptide: Ammonium transporter Rh type A
    • Protein or peptide: Ankyrin-1
    • Protein or peptide: Band 3 anion transport protein
    • Protein or peptide: Protein 4.2
    • Protein or peptide: Glycophorin-A
  • Ligand: CHOLESTEROL
  • Ligand: Digitonin
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: DIUNDECYL PHOSPHATIDYL CHOLINE
  • Ligand: [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate
  • Ligand: water

+
Supramolecule #1: Band 3 anion exchanger complexed with glycophorin A, in outward f...

SupramoleculeName: Band 3 anion exchanger complexed with glycophorin A, in outward facing state
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6
Details: Particle set isolated by 3D classification from mixture mostly containing ankyrin complexes.
Source (natural)Organism: Homo sapiens (human) / Organ: Blood / Tissue: Erythrocytes / Location in cell: Plasma membrane

+
Macromolecule #1: Blood group Rh(CE) polypeptide

MacromoleculeName: Blood group Rh(CE) polypeptide / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 45.598918 KDa
SequenceString: MSSKYPRSVR RCLPLWALTL EAALILLFYF FTHYDASLED QKGLVASYQV GQDLTVMAAL GLGFLTSNFR RHSWSSVAFN LFMLALGVQ WAILLDGFLS QFPPGKVVIT LFSIRLATMS AMSVLISAGA VLGKVNLAQL VVMVLVEVTA LGTLRMVISN I FNTDYHMN ...String:
MSSKYPRSVR RCLPLWALTL EAALILLFYF FTHYDASLED QKGLVASYQV GQDLTVMAAL GLGFLTSNFR RHSWSSVAFN LFMLALGVQ WAILLDGFLS QFPPGKVVIT LFSIRLATMS AMSVLISAGA VLGKVNLAQL VVMVLVEVTA LGTLRMVISN I FNTDYHMN LRHFYVFAAY FGLTVAWCLP KPLPKGTEDN DQRATIPSLS AMLGALFLWM FWPSVNSPLL RSPIQRKNAM FN TYYALAV SVVTAISGSS LAHPQRKISM TYVHSAVLAG GVAVGTSCHL IPSPWLAMVL GLVAGLISIG GAKCLPVCCN RVL GIHHIS VMHSIFSLLG LLGEITYIVL LVLHTVWNGN GMIGFQVLLS IGELSLAIVI ALTSGLLTGL LLNLKIWKAP HVAK YFDDQ VFWKFPHLAV GF

UniProtKB: Blood group Rh(CE) polypeptide

+
Macromolecule #2: Ammonium transporter Rh type A

MacromoleculeName: Ammonium transporter Rh type A / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 44.229629 KDa
SequenceString: MRFTFPLMAI VLEIAMIVLF GLFVEYETDQ TVLEQLNITK PTDMGIFFEL YPLFQDVHVM IFVGFGFLMT FLKKYGFSSV GINLLVAAL GLQWGTIVQG ILQSQGQKFN IGIKNMINAD FSAATVLISF GAVLGKTSPT QMLIMTILEI VFFAHNEYLV S EIFKASDI ...String:
MRFTFPLMAI VLEIAMIVLF GLFVEYETDQ TVLEQLNITK PTDMGIFFEL YPLFQDVHVM IFVGFGFLMT FLKKYGFSSV GINLLVAAL GLQWGTIVQG ILQSQGQKFN IGIKNMINAD FSAATVLISF GAVLGKTSPT QMLIMTILEI VFFAHNEYLV S EIFKASDI GASMTIHAFG AYFGLAVAGI LYRSGLRKGH ENEESAYYSD LFAMIGTLFL WMFWPSFNSA IAEPGDKQCR AI VNTYFSL AACVLTAFAF SSLVEHRGKL NMVHIQNATL AGGVAVGTCA DMAIHPFGSM IIGSIAGMVS VLGYKFLTPL FTT KLRIHD TCGVHNLHGL PGVVGGLAGI VAVAMGASNT SMAMQAAALG SSIGTAVVGG LMTGLILKLP LWGQPSDQNC YDDS VYWKV PKTR

UniProtKB: Ammonium transporter Rh type A

+
Macromolecule #3: Ankyrin-1

MacromoleculeName: Ankyrin-1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 206.522625 KDa
SequenceString: MPYSVGFREA DAATSFLRAA RSGNLDKALD HLRNGVDINT CNQNGLNGLH LASKEGHVKM VVELLHKEII LETTTKKGNT ALHIAALAG QDEVVRELVN YGANVNAQSQ KGFTPLYMAA QENHLEVVKF LLENGANQNV ATEDGFTPLA VALQQGHENV V AHLINYGT ...String:
MPYSVGFREA DAATSFLRAA RSGNLDKALD HLRNGVDINT CNQNGLNGLH LASKEGHVKM VVELLHKEII LETTTKKGNT ALHIAALAG QDEVVRELVN YGANVNAQSQ KGFTPLYMAA QENHLEVVKF LLENGANQNV ATEDGFTPLA VALQQGHENV V AHLINYGT KGKVRLPALH IAARNDDTRT AAVLLQNDPN PDVLSKTGFT PLHIAAHYEN LNVAQLLLNR GASVNFTPQN GI TPLHIAS RRGNVIMVRL LLDRGAQIET KTKDELTPLH CAARNGHVRI SEILLDHGAP IQAKTKNGLS PIHMAAQGDH LDC VRLLLQ YDAEIDDITL DHLTPLHVAA HCGHHRVAKV LLDKGAKPNS RALNGFTPLH IACKKNHVRV MELLLKTGAS IDAV TESGL TPLHVASFMG HLPIVKNLLQ RGASPNVSNV KVETPLHMAA RAGHTEVAKY LLQNKAKVNA KAKDDQTPLH CAARI GHTN MVKLLLENNA NPNLATTAGH TPLHIAAREG HVETVLALLE KEASQACMTK KGFTPLHVAA KYGKVRVAEL LLERDA HPN AAGKNGLTPL HVAVHHNNLD IVKLLLPRGG SPHSPAWNGY TPLHIAAKQN QVEVARSLLQ YGGSANAESV QGVTPLH LA AQEGHAEMVA LLLSKQANGN LGNKSGLTPL HLVAQEGHVP VADVLIKHGV MVDATTRMGY TPLHVASHYG NIKLVKFL L QHQADVNAKT KLGYSPLHQA AQQGHTDIVT LLLKNGASPN EVSSDGTTPL AIAKRLGYIS VTDVLKVVTD ETSFVLVSD KHRMSFPETV DEILDVSEDE GEELISFKAE RRDSRDVDEE KELLDFVPKL DQVVESPAIP RIPCAMPETV VIRSEEQEQA SKEYDEDSL IPSSPATETS DNISPVASPV HTGFLVSFMV DARGGSMRGS RHNGLRVVIP PRTCAAPTRI TCRLVKPQKL S TPPPLAEE EGLASRIIAL GPTGAQFLSP VIVEIPHFAS HGRGDRELVV LRSENGSVWK EHRSRYGESY LDQILNGMDE EL GSLEELE KKRVCRIITT DFPLYFVIMS RLCQDYDTIG PEGGSLKSKL VPLVQATFPE NAVTKRVKLA LQAQPVPDEL VTK LLGNQA TFSPIVTVEP RRRKFHRPIG LRIPLPPSWT DNPRDSGEGD TTSLRLLCSV IGGTDQAQWE DITGTTKLVY ANEC ANFTT NVSARFWLSD CPRTAEAVNF ATLLYKELTA VPYMAKFVIF AKMNDPREGR LRCYCMTDDK VDKTLEQHEN FVEVA RSRD IEVLEGMSLF AELSGNLVPV KKAAQQRSFH FQSFRENRLA MPVKVRDSSR EPGGSLSFLR KAMKYEDTQH ILCHLN ITM PPCAKGSGAE DRRRTPTPLA LRYSILSEST PGSLSGTEQA EMKMAVISEH LGLSWAELAR ELQFSVEDIN RIRVENP NS LLEQSVALLN LWVIREGQNA NMENLYTALQ SIDRGEIVNM LEGSGRQSRN LKPDRRHTDR DYSLSPSQMN GYSSLQDE L LSPASLGCAL SSPLRADQYW NEVAVLDAIP LAATEHDTML EMSDMQVWSA GLTPSLVTAE DSSLECSKAE DSDATGHEW KLEGALSEEP RGPELGSLEL VEDDTVDSDA TNGLIDLLEQ EEGQRSEEKL PGSKRQDDAT GAGQDSENEV SLVSGHQRGQ ARITHSPTV SQVTERSQDR LQDWDADGSI VSYLQDAAQG SWQEEVTQGP HSFQGTSTMT EGLEPGGSQE YEKVLVSVSE H TWTEQPEA ESSQADRDRR QQGQEEQVQE AKNTFTQVVQ GNEFQNIPGE QVTEEQFTDE QGNIVTKKII RKVVRQIDLS SA DAAQEHE EVTVEGPLED PSELEVDIDY FMKHSKDHTS TPNP

UniProtKB: Ankyrin-1

+
Macromolecule #4: Band 3 anion transport protein

MacromoleculeName: Band 3 anion transport protein / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 101.883859 KDa
SequenceString: MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS HPGTHKVYVE LQELVMDEKN QELRWMEAAR WVQLEENLG ENGAWGRPHL SHLTFWSLLE LRRVFTKGTV LLDLQETSLA GVANQLLDRF IFEDQIRPQD REELLRALLL K HSHAGELE ...String:
MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS HPGTHKVYVE LQELVMDEKN QELRWMEAAR WVQLEENLG ENGAWGRPHL SHLTFWSLLE LRRVFTKGTV LLDLQETSLA GVANQLLDRF IFEDQIRPQD REELLRALLL K HSHAGELE ALGGVKPAVL TRSGDPSQPL LPQHSSLETQ LFCEQGDGGT EGHSPSGILE KIPPDSEATL VLVGRADFLE QP VLGFVRL QEAAELEAVE LPVPIRFLFV LLGPEAPHID YTQLGRAAAT LMSERVFRID AYMAQSRGEL LHSLEGFLDC SLV LPPTDA PSEQALLSLV PVQRELLRRR YQSSPAKPDS SFYKGLDLNG GPDDPLQQTG QLFGGLVRDI RRRYPYYLSD ITDA FSPQV LAAVIFIYFA ALSPAITFGG LLGEKTRNQM GVSELLISTA VQGILFALLG AQPLLVVGFS GPLLVFEEAF FSFCE TNGL EYIVGRVWIG FWLILLVVLV VAFEGSFLVR FISRYTQEIF SFLISLIFIY ETFSKLIKIF QDHPLQKTYN YNVLMV PKP QGPLPNTALL SLVLMAGTFF FAMMLRKFKN SSYFPGKLRR VIGDFGVPIS ILIMVLVDFF IQDTYTQKLS VPDGFKV SN SSARGWVIHP LGLRSEFPIW MMFASALPAL LVFILIFLES QITTLIVSKP ERKMVKGSGF HLDLLLVVGM GGVAALFG M PWLSATTVRS VTHANALTVM GKASTPGAAA QIQEVKEQRI SGLLVAVLVG LSILMEPILS RIPLAVLFGI FLYMGVTSL SGIQLFDRIL LLFKPPKYHP DVPYVKRVKT WRMHLFTGIQ IICLAVLWVV KSTPASLALP FVLILTVPLR RVLLPLIFRN VELQCLDAD DAKATFDEEE GRDEYDEVAM PV

UniProtKB: Band 3 anion transport protein

+
Macromolecule #5: Protein 4.2

MacromoleculeName: Protein 4.2 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 77.096914 KDa
SequenceString: MGQALGIKSC DFQAARNNEE HHTKALSSRR LFVRRGQPFT IILYFRAPVR AFLPALKKVA LTAQTGEQPS KINRTQATFP ISSLGDRKW WSAVVEERDA QSWTISVTTP ADAVIGHYSL LLQVSGRKQL LLGQFTLLFN PWNREDAVFL KNEAQRMEYL L NQNGLIYL ...String:
MGQALGIKSC DFQAARNNEE HHTKALSSRR LFVRRGQPFT IILYFRAPVR AFLPALKKVA LTAQTGEQPS KINRTQATFP ISSLGDRKW WSAVVEERDA QSWTISVTTP ADAVIGHYSL LLQVSGRKQL LLGQFTLLFN PWNREDAVFL KNEAQRMEYL L NQNGLIYL GTADCIQAES WDFGQFEGDV IDLSLRLLSK DKQVEKWSQP VHVARVLGAL LHFLKEQRVL PTPQTQATQE GA LLNKRRG SVPILRQWLT GRGRPVYDGQ AWVLAAVACT VLRCLGIPAR VVTTFASAQG TGGRLLIDEY YNEEGLQNGE GQR GRIWIF QTSTECWMTR PALPQGYDGW QILHPSAPNG GGVLGSCDLV PVRAVKEGTL GLTPAVSDLF AAINASCVVW KCCE DGTLE LTDSNTKYVG NNISTKGVGS DRCEDITQNY KYPEGSLQEK EVLERVEKEK MEREKDNGIR PPSLETASPL YLLLK APSS LPLRGDAQIS VTLVNHSEQE KAVQLAIGVQ AVHYNGVLAA KLWRKKLHLT LSANLEKIIT IGLFFSNFER NPPENT FLR LTAMATHSES NLSCFAQEDI AICRPHLAIK MPEKAEQYQP LTASVSLQNS LDAPMEDCVI SILGRGLIHR ERSYRFR SV WPENTMCAKF QFTPTHVGLQ RLTVEVDCNM FQNLTNYKSV TVVAPELSA

UniProtKB: Protein 4.2

+
Macromolecule #6: Glycophorin-A

MacromoleculeName: Glycophorin-A / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.348433 KDa
SequenceString:
MYGKIIFVLL LSEIVSISAS STTGVAMHTS TSSSVTKSYI SSQTNDTHKR DTYAATPRAH EVSEISVRTV YPPEEETGER VQLAHHFSE PEITLIIFGV MAGVIGTILL ISYGIRRLIK KSPSDVKPLP SPDTDVPLSS VEIENPETSD Q

UniProtKB: Glycophorin-A

+
Macromolecule #7: CHOLESTEROL

MacromoleculeName: CHOLESTEROL / type: ligand / ID: 7 / Number of copies: 6 / Formula: CLR
Molecular weightTheoretical: 386.654 Da
Chemical component information

ChemComp-CLR:
CHOLESTEROL

+
Macromolecule #8: Digitonin

MacromoleculeName: Digitonin / type: ligand / ID: 8 / Number of copies: 2 / Formula: AJP
Molecular weightTheoretical: 1.229312 KDa
Chemical component information

ChemComp-AJP:
Digitonin / detergent*YM

+
Macromolecule #9: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 9 / Number of copies: 2 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

+
Macromolecule #10: DIUNDECYL PHOSPHATIDYL CHOLINE

MacromoleculeName: DIUNDECYL PHOSPHATIDYL CHOLINE / type: ligand / ID: 10 / Number of copies: 2 / Formula: PLC
Molecular weightTheoretical: 622.834 Da
Chemical component information

ChemComp-PLC:
DIUNDECYL PHOSPHATIDYL CHOLINE / phospholipid*YM

+
Macromolecule #11: [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(o...

MacromoleculeName: [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate
type: ligand / ID: 11 / Number of copies: 2 / Formula: PIO
Molecular weightTheoretical: 746.566 Da
Chemical component information

ChemComp-PIO:
[(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate

+
Macromolecule #12: water

MacromoleculeName: water / type: ligand / ID: 12 / Number of copies: 554 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration8 mg/mL
BufferpH: 7.4
Details: Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v ...Details: Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification.
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: 4-6 seconds, wait time 30 seconds.
DetailsAnkyrin complex mixture purified from digitonin-solubilized erythrocyte ghost membranes

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 2 / Number real images: 14464 / Average exposure time: 2.5 sec. / Average electron dose: 58.0 e/Å2 / Details: Two grids were imaged in a single session.
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.5 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: Generated by stochastic gradient descent using ab intio reconstruction job type in cryoSPARC v3.
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3)
Details: Main map corresponds to a composite map of EMD-26916 (RhAG/CE+ankyrin-1 (AR1-5), EMD-26917 (Protein 4.2), EMD-26918 (Ankyrin-1), EMD-26919 (Band3-I cytoplasmic domains), EMD-26940 (Band3-I ...Details: Main map corresponds to a composite map of EMD-26916 (RhAG/CE+ankyrin-1 (AR1-5), EMD-26917 (Protein 4.2), EMD-26918 (Ankyrin-1), EMD-26919 (Band3-I cytoplasmic domains), EMD-26940 (Band3-I TM domains). The consensus global refinement is provided in additional maps.
Number images used: 710734
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3)
Final 3D classificationDetails: Consensus refinement of erythrocyte ankyrin-1 complexes
FSC plot (resolution estimation)

-
Atomic model buiding 1

Initial modelPDB ID:

4yzf


Chain - Chain ID: A / Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-7v0k:
Consensus refinement of human erythrocyte ankyrin-1 complex (Composite map)

+
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