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- EMDB-6864: The Cryo-EM Structure of Human Catalytic Step I Spliceosome (C co... -

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Entry
Database: EMDB / ID: 6864
TitleThe Cryo-EM Structure of Human Catalytic Step I Spliceosome (C complex) at 4.1 angstrom resolution
Map data
SampleHuman Catalytic Step I Spliceosome
  • Pre-mRNA-processing-splicing factor 8
  • (nucleic-acidNucleic acid) x 4
  • 116 kDa U5 small nuclear ribonucleoprotein component
  • (U5 small nuclear ribonucleoprotein ...) x 2
  • (Pre-mRNA-splicing factor ...) x 8
  • Crooked neck-like protein 1
  • Cell division cycle 5-like protein
  • Protein BUD31 homolog
  • Spliceosome-associated protein CWC15 homolog
  • SNW domain-containing protein 1
  • Peptidyl-prolyl cis-trans isomerase-like 1
  • Pleiotropic regulator 1
  • Intron-binding protein aquarius
  • Serine/arginine repetitive matrix protein 2
  • (Pre-mRNA-processing factor ...) x 2
  • Coiled-coil domain-containing protein 94
  • Eukaryotic initiation factor 4A-III
  • Protein mago nashi homolog 2
  • RNA-binding protein 8A
  • Protein CASC3
  • (Small nuclear ribonucleoprotein ...SnRNP) x 6
  • Small nuclear ribonucleoprotein-associated proteins B and B'
  • (U2 small nuclear ribonucleoprotein ...) x 2
  • (Peptidyl-prolyl cis-trans isomerase ...Prolyl isomerase) x 2
  • Peptidylprolyl isomerase domain and WD repeat-containing protein 1
  • UNKNOW
  • (ligand) x 6
Function / homologyTranscription factor, GTP-binding domain / RNA-binding motif protein 8 / DEAD/DEAH box helicase domain / LSM domain superfamily / Pre-mRNA-splicing factor Isy1 / Homeobox-like domain superfamily / Translation protein, beta-barrel domain superfamily / Pre-mRNA-splicing factor SPF27 / CWC16 protein / Tetratricopeptide-like helical domain superfamily ...Transcription factor, GTP-binding domain / RNA-binding motif protein 8 / DEAD/DEAH box helicase domain / LSM domain superfamily / Pre-mRNA-splicing factor Isy1 / Homeobox-like domain superfamily / Translation protein, beta-barrel domain superfamily / Pre-mRNA-splicing factor SPF27 / CWC16 protein / Tetratricopeptide-like helical domain superfamily / Helicase-associated domain / Pre-mRNA-splicing factor Cwf15/Cwc15 / Translation elongation factor EFG/EF2, domain IV / Small GTP-binding protein domain / Sec63 domain / Translation elongation factor EFTu-like, domain 2 / Domain of unknown function DUF1605 / Ribonuclease H-like superfamily / SKI-interacting protein SKIP, SNW domain / Pre-mRNA-splicing factor 19 / MIF4G-like domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Immunoglobulin E-set / Ribosomal protein S5 domain 2-type fold, subgroup / RNA helicase, DEAD-box type, Q motif / Helicase superfamily 1/2, ATP-binding domain / mRNA splicing factor SYF2 / PRO8NT domain / mRNA splicing factor Cwf21 domain / Zinc finger, RING/FYVE/PHD-type / Tetratricopeptide repeat-containing domain / PROCT domain / Nucleotide-binding alpha-beta plait domain superfamily / PROCN domain / Mago nashi protein / Initiation factor eIF-4 gamma, MA3 / Peptidyl-prolyl cis-trans isomerase E / PROCT (NUC072) domain / Breast carcinoma amplified sequence 2 (BCAS2) / Isy1-like splicing family / Oligonucleotide/oligosaccharide-binding (OB)-fold / PRO8NT (NUC069), PrP8 N-terminal domain / PROCN (NUC071) domain / Family of unknown function (DUF572) / SYF2 splicing factor / RNA recognition motif domain / cwf21 domain / Prp19/Pso4-like / CASC3/Barentsz eIF4AIII binding / N-terminal domain of CBF1 interacting co-repressor CIR / U6-snRNA interacting domain of PrP8 / U5-snRNA binding site 2 of PrP8 / Cwf15/Cwc15 cell cycle control protein / JAB1/MPN/MOV34 metalloenzyme domain / MIF4G-like, type 3 / WD40 repeat / U box domain / U2A'/phosphoprotein 32 family A, C-terminal / HAT (Half-A-TPR) repeat / DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain / G10 protein / Helicase, C-terminal / Zinc finger, CCCH-type / Leucine-rich repeat / LSM domain, eukaryotic/archaea-type / SANT/Myb domain / U-box domain / Ricin B, lectin domain / Elongation factor EFG, domain V-like / ATP-dependent RNA helicase DEAD-box, conserved site / Armadillo-type fold / Sm-like protein Lsm6/SmF / pre-mRNA splicing factor component / WD40-repeat-containing domain superfamily / Pre-mRNA-processing factor 19 / MPN domain / Pre-mRNA-splicing factor Isy1 superfamily / Zinc finger, CCCH-type superfamily / Mago nashi superfamily / Winged helix DNA-binding domain superfamily / RNA-binding domain superfamily / Elongation factor Tu GTP binding domain / C2 domain superfamily / 116kDa U5 small nuclear ribonucleoprotein component, C-terminal / EF-G domain III/V-like / U2 small nuclear ribonucleoprotein B'', RNA recognition motif 1 / U2 small nuclear ribonucleoprotein B'', RNA recognition motif 2 / Peptidyl-prolyl cis-trans isomerase E, RNA recognition motif / Pre-mRNA-splicing factor Cwc2/Slt11 / RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain) / Small nuclear ribonucleoprotein F / HAT (Half-A-TPR) repeat / Elongation factor G, domain IV / Elongation factor Tu domain 2 / Sec63 Brl domain / MA3 domain / Mago nashi protein / SKIP/SNW domain / LSM domain
Function and homology information
SourceHomo sapiens (human) / Human (human)
Methodsingle particle reconstruction / cryo EM / 4.1 Å resolution
AuthorsZhan X / Yan C / Zhang X / Lei J / Shi Y
CitationJournal: Science / Year: 2018
Title: Structure of a human catalytic step I spliceosome.
Authors: Xiechao Zhan / Chuangye Yan / Xiaofeng Zhang / Jianlin Lei / Yigong Shi
Abstract: Splicing by the spliceosome involves branching and exon ligation. The branching reaction leads to the formation of the catalytic step I spliceosome (C complex). Here we report the cryo-electron ...Splicing by the spliceosome involves branching and exon ligation. The branching reaction leads to the formation of the catalytic step I spliceosome (C complex). Here we report the cryo-electron microscopy structure of the human C complex at an average resolution of 4.1 angstroms. Compared with the C complex, the human complex contains 11 additional proteins. The step I splicing factors CCDC49 and CCDC94 (Cwc25 and Yju2 in , respectively) closely interact with the DEAH-family adenosine triphosphatase/helicase Prp16 and bridge the gap between Prp16 and the active-site RNA elements. These features, together with structural comparison of the human C and C* complexes, provide mechanistic insights into ribonucleoprotein remodeling and allow the proposition of a working mechanism for the C-to-C* transition.
Validation ReportPDB-ID: 5yzg

SummaryFull reportAbout validation report
DateDeposition: Dec 14, 2017 / Header (metadata) release: Aug 8, 2018 / Map release: Aug 8, 2018 / Last update: Aug 8, 2018

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.029
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.029
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: : PDB-5yzg
  • Surface level: 0.029
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic models: PDB-5yzg
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

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Map

Fileemd_6864.map.gz (map file in CCP4 format, 256001 KB)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
400 pix
1.34 Å/pix.
= 535.2 Å
400 pix
1.34 Å/pix.
= 535.2 Å
400 pix
1.34 Å/pix.
= 535.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.338 Å
Density
Contour Level:0.029 (by author), 0.029 (movie #1):
Minimum - Maximum-0.10495703 - 0.20941421
Average (Standard dev.)0.0008073554 (0.007974337)
Details

EMDB XML:

Space Group Number1
Map Geometry
Axis orderXYZ
Dimensions400400400
Origin0.0.0.
Limit399.399.399.
Spacing400400400
CellA=B=C: 535.2 Å
α=β=γ: 90.0 deg.

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.3381.3381.338
M x/y/z400400400
origin x/y/z0.0000.0000.000
length x/y/z535.200535.200535.200
α/β/γ90.00090.00090.000
start NX/NY/NZ
NX/NY/NZ
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS400400400
D min/max/mean-0.1050.2090.001

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Supplemental data

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Sample components

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Entire Human Catalytic Step I Spliceosome

EntireName: Human Catalytic Step I Spliceosome / Number of components: 52

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Component #1: protein, Human Catalytic Step I Spliceosome

ProteinName: Human Catalytic Step I Spliceosome / Recombinant expression: No
SourceSpecies: Homo sapiens (human)

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Component #2: protein, Pre-mRNA-processing-splicing factor 8

ProteinName: Pre-mRNA-processing-splicing factor 8 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 273.97425 kDa
SourceSpecies: Human (human)

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Component #3: nucleic-acid, U5 snRNA

Nucleic-acidName: U5 snRNAU5 spliceosomal RNA / Class: RNA / Structure: OTHER / Synthetic: No
Sequence:
AUACUCUGGU UUCUCUUCAG AUCGCAUAAA UCUUUCGCCU UUUACUAAAG AUUUCCGUGG AGAGGAACAA CUCUGAGUCU UAACCCAAUU UUUUGAGGCC UUGCUUUGGC AAGGCUA
MassTheoretical: 37.254855 kDa
SourceSpecies: Homo sapiens (human)

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Component #4: protein, 116 kDa U5 small nuclear ribonucleoprotein component

ProteinName: 116 kDa U5 small nuclear ribonucleoprotein component / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 109.560625 kDa
SourceSpecies: Human (human)

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Component #5: protein, U5 small nuclear ribonucleoprotein 200 kDa helicase

ProteinName: U5 small nuclear ribonucleoprotein 200 kDa helicase / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 244.823422 kDa
SourceSpecies: Human (human)

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Component #6: protein, U5 small nuclear ribonucleoprotein 40 kDa protein

ProteinName: U5 small nuclear ribonucleoprotein 40 kDa protein / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 39.359492 kDa
SourceSpecies: Human (human)

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Component #7: nucleic-acid, U6 snRNA

Nucleic-acidName: U6 snRNAU6 spliceosomal RNA / Class: RNA / Structure: OTHER / Synthetic: No
Sequence:
GUGCUCGCUU CGGCAGCACA UAUACUAAAA UUGGAACGAU ACAGAGAAGA UUAGCAUGGC CCCUGCGCAA GGAUGACACG CAAAUUCGUG AAGCGUUCCA UAUUUUU
MassTheoretical: 34.404438 kDa
SourceSpecies: Homo sapiens (human)

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Component #8: nucleic-acid, Pre-mRNA

Nucleic-acidName: Pre-mRNAPrimary transcript / Class: RNA / Structure: OTHER / Synthetic: No
Sequence:
GGGAAUACAC GGAAUUCGAG CUCGCCCACU CUUGGAUCGG AAACCCGUCG GCCUCCGAAC GNGUAAGAGC CUAGCAUGUA GAACUGGUUA CCUGCAGCCC AAGCUUGCGU ACACCAUCAG GGUACGUACU AGUACGUACA CCAUCAGGGU ACGGCUGCAC GUCUAGGGCG CAGUAGUCCA GGGUUUCCUU GAUGAUGUCA UACUUAUCCU GUCCCUUUUU UUUCCACGGC UCGCGGUUGA GGACAAACUC UUCGCGGUCU UUCCAGUGGG GAUCC
MassTheoretical: 88.08882 kDa
SourceSpecies: Human (human)

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Component #9: nucleic-acid, U2 snRNA

Nucleic-acidName: U2 snRNAU2 spliceosomal RNA / Class: RNA / Structure: OTHER / Synthetic: No
Sequence:
AUCGCUUCUC GGCCUUUUGG CUAAGAUCAA GUGUAGUAUC UGUUCUUAUC AGUUUAAUAU CUGAUACGUC CUCUAUCCGA GGACAAUAUA UUAAAUGGAU UUUUGGAGCA GGGAGAUGGA AUAGGAGCUU GCUCCGUCCA CUCCACGCAU CGACCUGGUA UUGCAGUACC UCCAGGAACG GUGCACCC
MassTheoretical: 60.186445 kDa
SourceSpecies: Homo sapiens (human)

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Component #10: protein, Pre-mRNA-splicing factor SYF1

ProteinName: Pre-mRNA-splicing factor SYF1 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 100.148711 kDa
SourceSpecies: Human (human)

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Component #11: protein, Crooked neck-like protein 1

ProteinName: Crooked neck-like protein 1 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 100.610008 kDa
SourceSpecies: Human (human)

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Component #12: protein, Pre-mRNA-splicing factor SPF27

ProteinName: Pre-mRNA-splicing factor SPF27 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 26.16342 kDa
SourceSpecies: Human (human)

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Component #13: protein, Cell division cycle 5-like protein

ProteinName: Cell division cycle 5-like protein / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 92.406883 kDa
SourceSpecies: Human (human)

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Component #14: protein, Pre-mRNA-splicing factor ISY1 homolog

ProteinName: Pre-mRNA-splicing factor ISY1 homolog / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 35.499074 kDa
SourceSpecies: Human (human)

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Component #15: protein, Pre-mRNA-splicing factor SYF2

ProteinName: Pre-mRNA-splicing factor SYF2 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 28.780518 kDa
SourceSpecies: Human (human)

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Component #16: protein, Protein BUD31 homolog

ProteinName: Protein BUD31 homolog / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 17.03285 kDa
SourceSpecies: Human (human)

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Component #17: protein, Pre-mRNA-splicing factor RBM22

ProteinName: Pre-mRNA-splicing factor RBM22 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 46.959555 kDa
SourceSpecies: Human (human)

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Component #18: protein, Spliceosome-associated protein CWC15 homolog

ProteinName: Spliceosome-associated protein CWC15 homolog / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 26.674447 kDa
SourceSpecies: Human (human)

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Component #19: protein, SNW domain-containing protein 1

ProteinName: SNW domain-containing protein 1 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 61.770648 kDa
SourceSpecies: Human (human)

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Component #20: protein, Peptidyl-prolyl cis-trans isomerase-like 1

ProteinName: Peptidyl-prolyl cis-trans isomerase-like 1 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 18.257805 kDa
SourceSpecies: Human (human)

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Component #21: protein, Pleiotropic regulator 1

ProteinName: Pleiotropic regulator 1 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 57.280758 kDa
SourceSpecies: Human (human)

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Component #22: protein, Intron-binding protein aquarius

ProteinName: Intron-binding protein aquarius / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 171.502453 kDa
SourceSpecies: Human (human)

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Component #23: protein, Serine/arginine repetitive matrix protein 2

ProteinName: Serine/arginine repetitive matrix protein 2 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 300.255312 kDa
SourceSpecies: Human (human)

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Component #24: protein, Pre-mRNA-splicing factor CWC22 homolog

ProteinName: Pre-mRNA-splicing factor CWC22 homolog / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 105.646578 kDa
SourceSpecies: Human (human)

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Component #25: protein, Pre-mRNA-processing factor 17

ProteinName: Pre-mRNA-processing factor 17 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 65.61218 kDa
SourceSpecies: Human (human)

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Component #26: protein, Pre-mRNA-splicing factor CWC25 homolog

ProteinName: Pre-mRNA-splicing factor CWC25 homolog / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 49.73682 kDa
SourceSpecies: Human (human)

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Component #27: protein, Coiled-coil domain-containing protein 94

ProteinName: Coiled-coil domain-containing protein 94 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 37.141816 kDa
SourceSpecies: Human (human)

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Component #28: protein, Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16

ProteinName: Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 140.720641 kDa
SourceSpecies: Human (human)

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Component #29: protein, Pre-mRNA-processing factor 19

ProteinName: Pre-mRNA-processing factor 19 / Number of Copies: 4 / Recombinant expression: No
MassTheoretical: 55.245547 kDa
SourceSpecies: Human (human)

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Component #30: protein, Eukaryotic initiation factor 4A-III

ProteinName: Eukaryotic initiation factor 4A-III / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 46.930961 kDa
SourceSpecies: Human (human)

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Component #31: protein, Protein mago nashi homolog 2

ProteinName: Protein mago nashi homolog 2 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 17.301799 kDa
SourceSpecies: Human (human)

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Component #32: protein, RNA-binding protein 8A

ProteinName: RNA-binding protein 8A / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 19.92507 kDa
SourceSpecies: Human (human)

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Component #33: protein, Protein CASC3

ProteinName: Protein CASC3 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 76.381992 kDa
SourceSpecies: Human (human)

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Component #34: protein, Small nuclear ribonucleoprotein Sm D3

ProteinName: Small nuclear ribonucleoprotein Sm D3 / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 13.940308 kDa
SourceSpecies: Human (human)

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Component #35: protein, Small nuclear ribonucleoprotein-associated proteins B and B'

ProteinName: Small nuclear ribonucleoprotein-associated proteins B and B'
Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 23.459688 kDa
SourceSpecies: Human (human)

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Component #36: protein, Small nuclear ribonucleoprotein Sm D1

ProteinName: Small nuclear ribonucleoprotein Sm D1 / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 13.310653 kDa
SourceSpecies: Human (human)

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Component #37: protein, Small nuclear ribonucleoprotein Sm D2

ProteinName: Small nuclear ribonucleoprotein Sm D2 / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 13.551928 kDa
SourceSpecies: Human (human)

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Component #38: protein, Small nuclear ribonucleoprotein F

ProteinName: Small nuclear ribonucleoprotein F / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 9.734171 kDa
SourceSpecies: Human (human)

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Component #39: protein, Small nuclear ribonucleoprotein E

ProteinName: Small nuclear ribonucleoprotein E / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 10.817601 kDa
SourceSpecies: Human (human)

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Component #40: protein, Small nuclear ribonucleoprotein G

ProteinName: Small nuclear ribonucleoprotein G / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 8.508084 kDa
SourceSpecies: Human (human)

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Component #41: protein, U2 small nuclear ribonucleoprotein A'

ProteinName: U2 small nuclear ribonucleoprotein A' / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 28.456584 kDa
SourceSpecies: Human (human)

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Component #42: protein, U2 small nuclear ribonucleoprotein B''

ProteinName: U2 small nuclear ribonucleoprotein B'' / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 25.524367 kDa
SourceSpecies: Human (human)

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Component #43: protein, Peptidyl-prolyl cis-trans isomerase E

ProteinName: Peptidyl-prolyl cis-trans isomerase E / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 33.475773 kDa
SourceSpecies: Human (human)

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Component #44: protein, Peptidylprolyl isomerase domain and WD repeat-containing...

ProteinName: Peptidylprolyl isomerase domain and WD repeat-containing protein 1
Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 73.679891 kDa
SourceSpecies: Human (human)

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Component #45: protein, Peptidyl-prolyl cis-trans isomerase G

ProteinName: Peptidyl-prolyl cis-trans isomerase G / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 88.854336 kDa
SourceSpecies: Human (human)

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Component #46: protein, UNKNOW

ProteinName: UNKNOW / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 2.631853 kDa
SourceSpecies: Homo sapiens (human)

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Component #47: ligand, INOSITOL 1,2,3,4,5,6-HEXAKISPHOSPHATE

LigandName: INOSITOL 1,2,3,4,5,6-HEXAKISPHOSPHATE / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 0.660035 kDa

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Component #48: ligand, GUANOSINE-5'-TRIPHOSPHATE

LigandName: GUANOSINE-5'-TRIPHOSPHATEGuanosine triphosphate / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 0.52318 kDa

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Component #49: ligand, MAGNESIUM ION

LigandName: MAGNESIUM ION / Number of Copies: 7 / Recombinant expression: No
MassTheoretical: 2.430505 MDa

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Component #50: ligand, ADENOSINE-5'-DIPHOSPHATE

LigandName: ADENOSINE-5'-DIPHOSPHATE / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 0.427201 kDa

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Component #51: ligand, ZINC ION

LigandName: ZINC ION / Number of Copies: 7 / Recombinant expression: No
MassTheoretical: 6.540905 MDa

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Component #52: ligand, ADENOSINE-5'-TRIPHOSPHATE

LigandName: ADENOSINE-5'-TRIPHOSPHATE / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 0.507181 kDa

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Experimental details

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Sample preparation

SpecimenSpecimen state: particle / Method: cryo EM
Sample solutionpH: 7.9
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
ImagingMicroscope: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 5 e/Å2 / Illumination mode: FLOOD BEAM
LensImaging mode: BRIGHT FIELD
Specimen HolderModel: FEI TITAN KRIOS AUTOGRID HOLDER
CameraDetector: GATAN K2 SUMMIT (4k x 4k)

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Image processing

ProcessingMethod: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 53633
3D reconstructionAlgorithm: FOURIER SPACE / Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF

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Atomic model buiding

Output model

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