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- EMDB-53554: Cryo-EM structure of the human pre-Bact-OTS complex (whole map) -

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Basic information

Entry
Database: EMDB / ID: EMD-53554
TitleCryo-EM structure of the human pre-Bact-OTS complex (whole map)
Map data
Sample
  • Complex: pre-Bact-OTS-complex
    • RNA: x 3 types
    • Protein or peptide: x 14 types
  • Ligand: x 1 types
Keywordsspliceosome / SPLICING
Function / homology
Function and homology information


microfibril / regulation of retinoic acid receptor signaling pathway / cis assembly of pre-catalytic spliceosome / regulation of vitamin D receptor signaling pathway / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / nuclear retinoic acid receptor binding / pre-mRNA binding / U2-type catalytic step 1 spliceosome / embryonic brain development / RNA splicing, via transesterification reactions ...microfibril / regulation of retinoic acid receptor signaling pathway / cis assembly of pre-catalytic spliceosome / regulation of vitamin D receptor signaling pathway / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / nuclear retinoic acid receptor binding / pre-mRNA binding / U2-type catalytic step 1 spliceosome / embryonic brain development / RNA splicing, via transesterification reactions / positive regulation of mRNA splicing, via spliceosome / mRNA 3'-end processing / positive regulation of vitamin D receptor signaling pathway / host-mediated activation of viral transcription / U2-type precatalytic spliceosome / mRNA cis splicing, via spliceosome / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / RNA polymerase binding / Notch binding / RUNX3 regulates NOTCH signaling / U2-type catalytic step 2 spliceosome / Transport of Mature mRNA derived from an Intron-Containing Transcript / U2-type spliceosomal complex / nuclear vitamin D receptor binding / NOTCH4 Intracellular Domain Regulates Transcription / transcription elongation factor activity / RNA Polymerase II Transcription Termination / NOTCH3 Intracellular Domain Regulates Transcription / : / Basigin interactions / K63-linked polyubiquitin modification-dependent protein binding / positive regulation of neurogenesis / nuclear androgen receptor binding / ubiquitin-ubiquitin ligase activity / precatalytic spliceosome / Notch-HLH transcription pathway / WW domain binding / Formation of paraxial mesoderm / ubiquitin-like protein conjugating enzyme binding / positive regulation of transforming growth factor beta receptor signaling pathway / SMAD binding / mRNA Splicing - Minor Pathway / spliceosomal tri-snRNP complex assembly / Prp19 complex / negative regulation of transcription elongation by RNA polymerase II / U5 snRNP / U5 snRNA binding / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / pre-mRNA intronic binding / U2 snRNA binding / U6 snRNA binding / Cajal body / U1 snRNA binding / U4/U6 x U5 tri-snRNP complex / retinoic acid receptor signaling pathway / cellular response to retinoic acid / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / acrosomal vesicle / positive regulation of protein export from nucleus / positive regulation of RNA splicing / nuclear receptor binding / helicase activity / protein localization to plasma membrane / spliceosomal complex / transcription coregulator activity / response to cocaine / positive regulation of transcription elongation by RNA polymerase II / sperm end piece / Downregulation of SMAD2/3:SMAD4 transcriptional activity / mRNA splicing, via spliceosome / positive regulation of protein import into nucleus / RING-type E3 ubiquitin transferase / Golgi lumen / Pre-NOTCH Transcription and Translation / NOTCH1 Intracellular Domain Regulates Transcription / cellular response to xenobiotic stimulus / cellular response to tumor necrosis factor / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / mRNA processing / nuclear matrix / protein tag activity / calcium-dependent protein binding / protein polyubiquitination / rRNA processing / osteoblast differentiation / transcription corepressor activity / ubiquitin protein ligase activity / single-stranded DNA binding / protein folding / sperm principal piece / microtubule cytoskeleton / cellular response to lipopolysaccharide / RNA polymerase II-specific DNA-binding transcription factor binding / transcription coactivator activity / RNA helicase activity / nuclear speck / cilium
Similarity search - Function
WW domain binding protein 11 / WW domain binding protein 11 / Peptidyl-prolyl cis-trans isomerase like 2, U-box domain / Ubiquitin-like modifier Hub1/Ubl5 / Pre-mRNA-splicing factor 38, C-terminal / Pre-mRNA-splicing factor 38-associated hydrophilic C-term / Micro-fibrillar-associated protein 1, C-terminal / Microfibrillar-associated protein 1 / Microfibril-associated/Pre-mRNA processing / U4/U6.U5 small nuclear ribonucleoprotein component Snu23 ...WW domain binding protein 11 / WW domain binding protein 11 / Peptidyl-prolyl cis-trans isomerase like 2, U-box domain / Ubiquitin-like modifier Hub1/Ubl5 / Pre-mRNA-splicing factor 38, C-terminal / Pre-mRNA-splicing factor 38-associated hydrophilic C-term / Micro-fibrillar-associated protein 1, C-terminal / Microfibrillar-associated protein 1 / Microfibril-associated/Pre-mRNA processing / U4/U6.U5 small nuclear ribonucleoprotein component Snu23 / Pre-mRNA-splicing factor 38 / Transcription elongation regulator 1-like / : / PRP38 family / TCERG1 WW domain / FF domain / : / RBM22 CCCH zinc finger domain / FF domain / FF domain superfamily / FF domain profile. / Contains two conserved F residues / Pre-mRNA-processing factor 17 / G10 protein signature 2. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase, cyclophilin A-like / BUD31/G10-related, conserved site / G10 protein signature 1. / : / STL11, N-terminal / SKI-interacting protein SKIP, SNW domain / SKI-interacting protein, SKIP / SKIP/SNW domain / Pre-mRNA-splicing factor Cwc2/Slt11 / G10 protein / Pre-mRNA-splicing factor BUD31 / Zinc-finger double-stranded RNA-binding / Zinc finger, double-stranded RNA binding / Brr2, N-terminal helicase PWI domain / : / N-terminal helicase PWI domain / Pre-mRNA-splicing helicase BRR2 plug domain / : / Winged Helix-turn-helix domain / Sec63 Brl domain / U-box domain profile. / Zinc finger, CCCH-type superfamily / : / zinc finger / 116kDa U5 small nuclear ribonucleoprotein component, N-terminal / 116kDa U5 small nuclear ribonucleoprotein component, C-terminal / Snu114, GTP-binding domain / 116 kDa U5 small nuclear ribonucleoprotein component N-terminus / Modified RING finger domain / U-box domain / Sec63 domain / Sec63 Brl domain / Matrin/U1-C-like, C2H2-type zinc finger / U1-like zinc finger / Zinc finger, CCCH-type / Zinc finger C3H1-type profile. / Elongation Factor G, domain II / Elongation Factor G, domain III / Translation elongation factor EFG/EF2, domain IV / Elongation factor G, domain IV / Elongation factor G, domain IV / Elongation factor G C-terminus / Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site / Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. / WW domain / WW/rsp5/WWP domain signature. / Elongation factor EFG, domain V-like / Elongation factor G C-terminus / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain profile. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain / Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD / Cyclophilin-like domain superfamily / PROCT domain / Prp8 RNase domain IV, fingers region / PROCT (NUC072) domain / PRO8NT domain / PROCN domain / Pre-mRNA-processing-splicing factor 8, U6-snRNA-binding / Pre-mRNA-processing-splicing factor 8, U5-snRNA-binding / RNA recognition motif, spliceosomal PrP8 / PRP8 domain IV core / WW domain superfamily / Pre-mRNA-processing-splicing factor 8, U5-snRNA-binding domain superfamily / Prp8 RNase domain IV, palm region / PRO8NT (NUC069), PrP8 N-terminal domain / PROCN (NUC071) domain / U6-snRNA interacting domain of PrP8 / U5-snRNA binding site 2 of PrP8 / RNA recognition motif of the spliceosomal PrP8 / PRP8 domain IV core / Pre-mRNA-processing-splicing factor 8 / EF-G domain III/V-like / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / WW domain / JAB1/Mov34/MPN/PAD-1 ubiquitin protease
Similarity search - Domain/homology
Transcription elongation regulator 1 / Pre-mRNA-processing factor 17 / U5 small nuclear ribonucleoprotein 200 kDa helicase / Protein BUD31 homolog / Microfibrillar-associated protein 1 / RING-type E3 ubiquitin-protein ligase PPIL2 / SNW domain-containing protein 1 / 116 kDa U5 small nuclear ribonucleoprotein component / Pre-mRNA-processing-splicing factor 8 / Pre-mRNA-splicing factor 38A ...Transcription elongation regulator 1 / Pre-mRNA-processing factor 17 / U5 small nuclear ribonucleoprotein 200 kDa helicase / Protein BUD31 homolog / Microfibrillar-associated protein 1 / RING-type E3 ubiquitin-protein ligase PPIL2 / SNW domain-containing protein 1 / 116 kDa U5 small nuclear ribonucleoprotein component / Pre-mRNA-processing-splicing factor 8 / Pre-mRNA-splicing factor 38A / Zinc finger matrin-type protein 2 / Ubiquitin-like protein 5 / Pre-mRNA-splicing factor RBM22 / WW domain-binding protein 11
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.12 Å
AuthorsZhang Z / Kumar V / Zhong J / Dybkov O / Kastner B / Urlaub H / Luhrmann R
Funding support Germany, 1 items
OrganizationGrant numberCountry
German Research Foundation (DFG) Germany
CitationJournal: To Be Published
Title: cryo-EM structure of the human pre-Bact-OTS complex
Authors: Zhang Z / Kumar V / Dybkov O / Zhong J / Kastner B / Henning U / Luehrmann R
History
DepositionMay 4, 2025-
Header (metadata) releaseMay 13, 2026-
Map releaseMay 13, 2026-
UpdateMay 13, 2026-
Current statusMay 13, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_53554.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.35 Å/pix.
x 400 pix.
= 540. Å
1.35 Å/pix.
x 400 pix.
= 540. Å
1.35 Å/pix.
x 400 pix.
= 540. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.35 Å
Density
Contour LevelBy AUTHOR: 0.055
Minimum - Maximum-0.16490501 - 0.35897565
Average (Standard dev.)0.00032380907 (±0.012297201)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 540.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_53554_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_53554_half_map_2.map
Projections & Slices
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Sample components

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Entire : pre-Bact-OTS-complex

EntireName: pre-Bact-OTS-complex
Components
  • Complex: pre-Bact-OTS-complex
    • RNA: U5 snRNA
    • RNA: U6 snRNA
    • Protein or peptide: U5 small nuclear ribonucleoprotein 200 kDa helicase
    • Protein or peptide: 116 kDa U5 small nuclear ribonucleoprotein component
    • Protein or peptide: Pre-mRNA-splicing factor 38A
    • Protein or peptide: Microfibrillar-associated protein 1
    • Protein or peptide: Protein BUD31 homolog
    • Protein or peptide: Transcription elongation regulator 1
    • Protein or peptide: WW domain-binding protein 11
    • RNA: pre-mRNA
    • Protein or peptide: Ubiquitin-like protein 5
    • Protein or peptide: Zinc finger matrin-type protein 2
    • Protein or peptide: Pre-mRNA-processing factor 17
    • Protein or peptide: Pre-mRNA-processing-splicing factor 8
    • Protein or peptide: Pre-mRNA-splicing factor RBM22
    • Protein or peptide: RING-type E3 ubiquitin-protein ligase PPIL2
    • Protein or peptide: SNW domain-containing protein 1
  • Ligand: INOSITOL HEXAKISPHOSPHATE

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Supramolecule #1: pre-Bact-OTS-complex

SupramoleculeName: pre-Bact-OTS-complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#17
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: U5 snRNA

MacromoleculeName: U5 snRNA / type: rna / ID: 1 / Number of copies: 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.496414 KDa
SequenceString:
ACUCUGGUUU CUCUUCAGAU CGCAUAAAUC UUUCGCCUUU UACUAAAGAU UUCCGUGGAG AGGAACAACU CUGAGUC

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Macromolecule #2: U6 snRNA

MacromoleculeName: U6 snRNA / type: rna / ID: 2 / Number of copies: 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 27.447449 KDa
SequenceString:
GUGCUCGCUU CGGCAGCACA UAUACUAAAA UUGGAACGAU ACAGAGAAGA UUAGCAUGGC CCCUGCGCAA GGAUGACACG CAAAA

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Macromolecule #10: pre-mRNA

MacromoleculeName: pre-mRNA / type: rna / ID: 10 / Number of copies: 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.307604 KDa
SequenceString:
GCCGCCAAGG UAUGUAUCAA GCUUACAAG

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Macromolecule #3: U5 small nuclear ribonucleoprotein 200 kDa helicase

MacromoleculeName: U5 small nuclear ribonucleoprotein 200 kDa helicase / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: RNA helicase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 244.823422 KDa
SequenceString: MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT RMGDKAQRTK PQMQEERRAK RRKRDEDRHD INKMKGYTL LSEGIDEMVG IIYKPKTKET RETYEVLLSF IQAALGDQPR DILCGAADEV LAVLKNEKLR DKERRKEIDL L LGQTDDTR ...String:
MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT RMGDKAQRTK PQMQEERRAK RRKRDEDRHD INKMKGYTL LSEGIDEMVG IIYKPKTKET RETYEVLLSF IQAALGDQPR DILCGAADEV LAVLKNEKLR DKERRKEIDL L LGQTDDTR YHVLVNLGKK ITDYGGDKEI QNMDDNIDET YGVNVQFESD EEEGDEDVYG EVREEASDDD MEGDEAVVRC TL SANLVAS GELMSSKKKD LHPRDIDAFW LQRQLSRFYD DAIVSQKKAD EVLEILKTAS DDRECENQLV LLLGFNTFDF IKV LRQHRM MILYCTLLAS AQSEAEKERI MGKMEADPEL SKFLYQLHET EKEDLIREER SRRERVRQSR MDTDLETMDL DQGG EALAP RQVLDLEDLV FTQGSHFMAN KRCQLPDGSF RRQRKGYEEV HVPALKPKPF GSEEQLLPVE KLPKYAQAGF EGFKT LNRI QSKLYRAALE TDENLLLCAP TGAGKTNVAL MCMLREIGKH INMDGTINVD DFKIIYIAPM RSLVQEMVGS FGKRLA TYG ITVAELTGDH QLCKEEISAT QIIVCTPEKW DIITRKGGER TYTQLVRLII LDEIHLLHDD RGPVLEALVA RAIRNIE MT QEDVRLIGLS ATLPNYEDVA TFLRVDPAKG LFYFDNSFRP VPLEQTYVGI TEKKAIKRFQ IMNEIVYEKI MEHAGKNQ V LVFVHSRKET GKTARAIRDM CLEKDTLGLF LREGSASTEV LRTEAEQCKN LELKDLLPYG FAIHHAGMTR VDRTLVEDL FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR WTELGALDIL QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPI ESQMVSKLPD MLNAEIVLGN VQNAKDAVNW LGYAYLYIRM LRSPTLYGIS HDDLKGDPLL DQRRLDLVHT A ALMLDKNN LVKYDKKTGN FQVTELGRIA SHYYITNDTV QTYNQLLKPT LSEIELFRVF SLSSEFKNIT VREEEKLELQ KL LERVPIP VKESIEEPSA KINVLLQAFI SQLKLEGFAL MADMVYVTQS AGRLMRAIFE IVLNRGWAQL TDKTLNLCKM IDK RMWQSM CPLRQFRKLP EEVVKKIEKK NFPFERLYDL NHNEIGELIR MPKMGKTIHK YVHLFPKLEL SVHLQPITRS TLKV ELTIT PDFQWDEKVH GSSEAFWILV EDVDSEVILH HEYFLLKAKY AQDEHLITFF VPVFEPLPPQ YFIRVVSDRW LSCET QLPV SFRHLILPEK YPPPTELLDL QPLPVSALRN SAFESLYQDK FPFFNPIQTQ VFNTVYNSDD NVFVGAPTGS GKTICA EFA ILRMLLQSSE GRCVYITPME ALAEQVYMDW YEKFQDRLNK KVVLLTGETS TDLKLLGKGN IIISTPEKWD ILSRRWK QR KNVQNINLFV VDEVHLIGGE NGPVLEVICS RMRYISSQIE RPIRIVALSS SLSNAKDVAH WLGCSATSTF NFHPNVRP V PLELHIQGFN ISHTQTRLLS MAKPVYHAIT KHSPKKPVIV FVPSRKQTRL TAIDILTTCA ADIQRQRFLH CTEKDLIPY LEKLSDSTLK ETLLNGVGYL HEGLSPMERR LVEQLFSSGA IQVVVASRSL CWGMNVAAHL VIIMDTQYYN GKIHAYVDYP IYDVLQMVG HANRPLQDDE GRCVIMCQGS KKDFFKKFLY EPLPVESHLD HCMHDHFNAE IVTKTIENKQ DAVDYLTWTF L YRRMTQNP NYYNLQGISH RHLSDHLSEL VEQTLSDLEQ SKCISIEDEM DVAPLNLGMI AAYYYINYTT IELFSMSLNA KT KVRGLIE IISNAAEYEN IPIRHHEDNL LRQLAQKVPH KLNNPKFNDP HVKTNLLLQA HLSRMQLSAE LQSDTEEILS KAI RLIQAC VDVLSSNGWL SPALAAMELA QMVTQAMWSK DSYLKQLPHF TSEHIKRCTD KGVESVFDIM EMEDEERNAL LQLT DSQIA DVARFCNRYP NIELSYEVVD KDSIRSGGPV VVLVQLEREE EVTGPVIAPL FPQKREEGWW VVIGDAKSNS LISIK RLTL QQKAKVKLDF VAPATGAHNY TLYFMSDAYM GCDQEYKFSV DVKEAETDSD SD

UniProtKB: U5 small nuclear ribonucleoprotein 200 kDa helicase

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Macromolecule #4: 116 kDa U5 small nuclear ribonucleoprotein component

MacromoleculeName: 116 kDa U5 small nuclear ribonucleoprotein component / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 109.560625 KDa
SequenceString: MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEMDDDD DDDDVGDHDD DHPGMEVVLH EDKKYYPTAE EVYGPEVETI VQEEDTQPL TEPIIKPVKT KKFTLMEQTL PVTVYEMDFL ADLMDNSELI RNVTLCGHLH HGKTCFVDCL IEQTHPEIRK R YDQDLCYT ...String:
MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEMDDDD DDDDVGDHDD DHPGMEVVLH EDKKYYPTAE EVYGPEVETI VQEEDTQPL TEPIIKPVKT KKFTLMEQTL PVTVYEMDFL ADLMDNSELI RNVTLCGHLH HGKTCFVDCL IEQTHPEIRK R YDQDLCYT DILFTEQERG VGIKSTPVTV VLPDTKGKSY LFNIMDTPGH VNFSDEVTAG LRISDGVVLF IDAAEGVMLN TE RLIKHAV QERLAVTVCI NKIDRLILEL KLPPTDAYYK LRHIVDEVNG LISMYSTDEN LILSPLLGNV CFSSSQYSIC FTL GSFAKI YADTFGDINY QEFAKRLWGD IYFNPKTRKF TKKAPTSSSQ RSFVEFILEP LYKILAQVVG DVDTSLPRTL DELG IHLTK EELKLNIRPL LRLVCKKFFG EFTGFVDMCV QHIPSPKVGA KPKIEHTYTG GVDSDLGEAM SDCDPDGPLM CHTTK MYST DDGVQFHAFG RVLSGTIHAG QPVKVLGENY TLEDEEDSQI CTVGRLWISV ARYHIEVNRV PAGNWVLIEG VDQPIV KTA TITEPRGNEE AQIFRPLKFN TTSVIKIAVE PVNPSELPKM LDGLRKVNKS YPSLTTKVEE SGEHVILGTG ELYLDCV MH DLRKMYSEID IKVADPVVTF CETVVETSSL KCFAETPNKK NKITMIAEPL EKGLAEDIEN EVVQITWNRK KLGEFFQT K YDWDLLAARS IWAFGPDATG PNILVDDTLP SEVDKALLGS VKDSIVQGFQ WGTREGPLCD ELIRNVKFKI LDAVVAQEP LHRGGGQIIP TARRVVYSAF LMATPRLMEP YYFVEVQAPA DCVSAVYTVL ARRRGHVTQD APIPGSPLYT IKAFIPAIDS FGFETDLRT HTQGQAFSLS VFHHWQIVPG DPLDKSIVIR PLEPQPAPHL AREFMIKTRR RKGLSEDVSI SKFFDDPMLL E LAKQDVVL NYPM

UniProtKB: 116 kDa U5 small nuclear ribonucleoprotein component

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Macromolecule #5: Pre-mRNA-splicing factor 38A

MacromoleculeName: Pre-mRNA-splicing factor 38A / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 37.563863 KDa
SequenceString: MANRTVKDAH SIHGTNPQYL VEKIIRTRIY ESKYWKEECF GLTAELVVDK AMELRFVGGV YGGNIKPTPF LCLTLKMLQI QPEKDIIVE FIKNEDFKYV RMLGALYMRL TGTAIDCYKY LEPLYNDYRK IKSQNRNGEF ELMHVDEFID ELLHSERVCD I ILPRLQKR ...String:
MANRTVKDAH SIHGTNPQYL VEKIIRTRIY ESKYWKEECF GLTAELVVDK AMELRFVGGV YGGNIKPTPF LCLTLKMLQI QPEKDIIVE FIKNEDFKYV RMLGALYMRL TGTAIDCYKY LEPLYNDYRK IKSQNRNGEF ELMHVDEFID ELLHSERVCD I ILPRLQKR YVLEEAEQLE PRVSALEEDM DDVESSEEEE EEDEKLERVP SPDHRRRSYR DLDKPRRSPT LRYRRSRSRS PR RRSRSPK RRSPSPRRER HRSKSPRRHR SRSRDRRHRS RSKSPGHHRS HRHRSHSKSP ERSKKSHKKS RRGNE

UniProtKB: Pre-mRNA-splicing factor 38A

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Macromolecule #6: Microfibrillar-associated protein 1

MacromoleculeName: Microfibrillar-associated protein 1 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 52.050527 KDa
SequenceString: MSVPSALMKQ PPIQSTAGAV PVRNEKGEIS MEKVKVKRYV SGKRPDYAPM ESSDEEDEEF QFIKKAKEQE AEPEEQEEDS SSDPRLRRL QNRISEDVEE RLARHRKIVE PEVVGESDSE VEGDAWRMER EDSSEEEEEE IDDEEIERRR GMMRQRAQER K NEEMEVME ...String:
MSVPSALMKQ PPIQSTAGAV PVRNEKGEIS MEKVKVKRYV SGKRPDYAPM ESSDEEDEEF QFIKKAKEQE AEPEEQEEDS SSDPRLRRL QNRISEDVEE RLARHRKIVE PEVVGESDSE VEGDAWRMER EDSSEEEEEE IDDEEIERRR GMMRQRAQER K NEEMEVME VEDEGRSGEE SESESEYEEY TDSEDEMEPR LKPVFIRKKD RVTVQEREAE ALKQKELEQE AKRMAEERRK YT LKIVEEE TKKELEENKR SLAALDALNT DDENDEEEYE AWKVRELKRI KRDREDREAL EKEKAEIERM RNLTEEERRA ELR ANGKVI TNKAVKGKYK FLQKYYHRGA FFMDEDEEVY KRDFSAPTLE DHFNKTILPK VMQVKNFGRS GRTKYTHLVD QDTT SFDSA WGQESAQNTK FFKQKAAGVR DVFERPSAKK RKTT

UniProtKB: Microfibrillar-associated protein 1

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Macromolecule #7: Protein BUD31 homolog

MacromoleculeName: Protein BUD31 homolog / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.03285 KDa
SequenceString:
MPKVKRSRKA PPDGWELIEP TLDELDQKMR EAETEPHEGK RKVESLWPIF RIHHQKTRYI FDLFYKRKAI SRELYEYCIK EGYADKNLI AKWKKQGYEN LCCLRCIQTR DTNFGTNCIC RVPKSKLEVG RIIECTHCGC RGCSG

UniProtKB: Protein BUD31 homolog

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Macromolecule #8: Transcription elongation regulator 1

MacromoleculeName: Transcription elongation regulator 1 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 124.083 KDa
SequenceString: MAERGGDGGE SERFNPGELR MAQQQALRFR GPAPPPNAVM RGPPPLMRPP PPFGMMRGPP PPPRPPFGRP PFDPNMPPMP PPGGIPPPM GPPHLQRPPF MPPPMSSMPP PPGMMFPPGM PPVTAPGTPA LPPTEEIWVE NKTPDGKVYY YNARTRESAW T KPDGVKVI ...String:
MAERGGDGGE SERFNPGELR MAQQQALRFR GPAPPPNAVM RGPPPLMRPP PPFGMMRGPP PPPRPPFGRP PFDPNMPPMP PPGGIPPPM GPPHLQRPPF MPPPMSSMPP PPGMMFPPGM PPVTAPGTPA LPPTEEIWVE NKTPDGKVYY YNARTRESAW T KPDGVKVI QQSELTPMLA AQAQVQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQ AQVQAQV QAQVQAQAVG ASTPTTSSPA PAVSTSTSSS TPSSTTSTTT TATSVAQTVS TPTTQDQTPS SAVSVATPTV SVS TPAPTA TPVQTVPQPH PQTLPPAVPH SVPQPTTAIP AFPPVMVPPF RVPLPGMPIP LPGVAMMQIV SCPYVKTVAT TKTG VLPGM APPIVPMIHP QVAIAASPAT LAGATAVSEW TEYKTADGKT YYYNNRTLES TWEKPQELKE KEKLEEKIKE PIKEP SEEP LPMETEEEDP KEEPIKEIKE EPKEEEMTEE EKAAQKAKPV ATAPIPGTPW CVVWTGDERV FFYNPTTRLS MWDRPD DLI GRADVDKIIQ EPPHKKGMEE LKKLRHPTPT MLSIQKWQFS MSAIKEEQEL MEEINEDEPV KAKKRKRDDN KDIDSEK EA AMEAEIKAAR ERAIVPLEAR MKQFKDMLLE RGVSAFSTWE KELHKIVFDP RYLLLNPKER KQVFDQYVKT RAEEERRE K KNKIMQAKED FKKMMEEAKF NPRATFSEFA AKHAKDSRFK AIEKMKDREA LFNEFVAAAR KKEKEDSKTR GEKIKSDFF ELLSNHHLDS QSRWSKVKDK VESDPRYKAV DSSSMREDLF KQYIEKIAKN LDSEKEKELE RQARIEASLR EREREVQKAR SEQTKEIDR EREQHKREEA IQNFKALLSD MVRSSDVSWS DTRRTLRKDH RWESGSLLER EEKEKLFNEH IEALTKKKRE H FRQLLDET SAITLTSTWK EVKKIIKEDP RCIKFSSSDR KKQREFEEYI RDKYITAKAD FRTLLKETKF ITYRSKKLIQ ES DQHLKDV EKILQNDKRY LVLDCVPEER RKLIVAYVDD LDRRGPPPPP TASEPTRRST K

UniProtKB: Transcription elongation regulator 1

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Macromolecule #9: WW domain-binding protein 11

MacromoleculeName: WW domain-binding protein 11 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 70.098641 KDa
SequenceString: MGRRSTSSTK SGKFMNPTDQ ARKEARKREL KKNKKQRMMV RAAVLKMKDP KQIIRDMEKL DEMEFNPVQQ PQLNEKVLKD KRKKLRETF ERILRLYEKE NPDIYKELRK LEVEYEQKRA QLSQYFDAVK NAQHVEVESI PLPDMPHAPS NILIQDIPLP G AQPPSILK ...String:
MGRRSTSSTK SGKFMNPTDQ ARKEARKREL KKNKKQRMMV RAAVLKMKDP KQIIRDMEKL DEMEFNPVQQ PQLNEKVLKD KRKKLRETF ERILRLYEKE NPDIYKELRK LEVEYEQKRA QLSQYFDAVK NAQHVEVESI PLPDMPHAPS NILIQDIPLP G AQPPSILK KTSAYGPPTR AVSILPLLGH GVPRLPPGRK PPGPPPGPPP PQVVQMYGRK VGFALDLPPR RRDEDMLYSP EL AQRGHDD DVSSTSEDDG YPEDMDQDKH DDSTDDSDTD KSDGESDGDE FVHRDNGERD NNEEKKSGLS VRFADMPGKS RKK KKNMKE LTPLQAMMLR MAGQEIPEEG REVEEFSEDD DEDDSDDSEA EKQSQKQHKE ESHSDGTSTA SSQQQAPPQS VPPS QIQAP PMPGPPPLGP PPAPPLRPPG PPTGLPPGPP PGAPPFLRPP GMPGLRGPLP RLLPPGPPPG RPPGPPPGPP PGLPP GPPP RGPPPRLPPP APPGIPPPRP GMMRPPLVPP LGPAPPGLFP PAPLPNPGVL SAPPNLIQRP KADDTSAATI EKKATA TIS AKPQITNPKA EITRFVPTAL RVRRENKGAT AAPQRKSEDD SAVPLAKAAP KSGPSVPVSV QTKDDVYEAF MKEMEGL L

UniProtKB: WW domain-binding protein 11

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Macromolecule #11: Ubiquitin-like protein 5

MacromoleculeName: Ubiquitin-like protein 5 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.560945 KDa
SequenceString:
MIEVVCNDRL GKKVRVKCNT DDTIGDLKKL IAAQTGTRWN KIVLKKWYTI FKDHVSLGDY EIHDGMNLEL YYQ

UniProtKB: Ubiquitin-like protein 5

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Macromolecule #12: Zinc finger matrin-type protein 2

MacromoleculeName: Zinc finger matrin-type protein 2 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 23.664047 KDa
SequenceString: MASGSGTKNL DFRRKWDKDE YEKLAEKRLT EEREKKDGKP VQPVKRELLR HRDYKVDLES KLGKTIVITK TTPQSEMGGY YCNVCDCVV KDSINFLDHI NGKKHQRNLG MSMRVERSTL DQVKKRFEVN KKKMEEKQKD YDFEERMKEL REEEEKAKAY K KEKQKEKK ...String:
MASGSGTKNL DFRRKWDKDE YEKLAEKRLT EEREKKDGKP VQPVKRELLR HRDYKVDLES KLGKTIVITK TTPQSEMGGY YCNVCDCVV KDSINFLDHI NGKKHQRNLG MSMRVERSTL DQVKKRFEVN KKKMEEKQKD YDFEERMKEL REEEEKAKAY K KEKQKEKK RRAEEDLTFE EDDEMAAVMG FSGFGSTKKS Y

UniProtKB: Zinc finger matrin-type protein 2

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Macromolecule #13: Pre-mRNA-processing factor 17

MacromoleculeName: Pre-mRNA-processing factor 17 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 65.61218 KDa
SequenceString: MSAAIAALAA SYGSGSGSES DSDSESSRCP LPAADSLMHL TKSPSSKPSL AVAVDSAPEV AVKEDLETGV HLDPAVKEVQ YNPTYETMF APEFGPENPF RTQQMAAPRN MLSGYAEPAH INDFMFEQQR RTFATYGYAL DPSLDNHQVS AKYIGSVEEA E KNQGLTVF ...String:
MSAAIAALAA SYGSGSGSES DSDSESSRCP LPAADSLMHL TKSPSSKPSL AVAVDSAPEV AVKEDLETGV HLDPAVKEVQ YNPTYETMF APEFGPENPF RTQQMAAPRN MLSGYAEPAH INDFMFEQQR RTFATYGYAL DPSLDNHQVS AKYIGSVEEA E KNQGLTVF ETGQKKTEKR KKFKENDASN IDGFLGPWAK YVDEKDVAKP SEEEQKELDE ITAKRQKKGK QEEEKPGEEK TI LHVKEMY DYQGRSYLHI PQDVGVNLRS TMPPEKCYLP KKQIHVWSGH TKGVSAVRLF PLSGHLLLSC SMDCKIKLWE VYG ERRCLR TFIGHSKAVR DICFNTAGTQ FLSAAYDRYL KLWDTETGQC ISRFTNRKVP YCVKFNPDED KQNLFVAGMS DKKI VQWDI RSGEIVQEYD RHLGAVNTIV FVDENRRFVS TSDDKSLRVW EWDIPVDFKY IAEPSMHSMP AVTLSPNGKW LACQS MDNQ ILIFGAQNRF RLNKKKIFKG HMVAGYACQV DFSPDMSYVI SGDGNGKLNI WDWKTTKLYS RFKAHDKVCI GAVWHP HET SKVITCGWDG LIKLWD

UniProtKB: Pre-mRNA-processing factor 17

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Macromolecule #14: Pre-mRNA-processing-splicing factor 8

MacromoleculeName: Pre-mRNA-processing-splicing factor 8 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 273.97425 KDa
SequenceString: MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK FGFVDAQKED MPPEHVRKII RDHGDMTNRK FRHDKRVYL GALKYMPHAV LKLLENMPMP WEQIRDVPVL YHITGAISFV NEIPWVIEPV YISQWGSMWI MMRREKRDRR H FKRMRFPP ...String:
MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK FGFVDAQKED MPPEHVRKII RDHGDMTNRK FRHDKRVYL GALKYMPHAV LKLLENMPMP WEQIRDVPVL YHITGAISFV NEIPWVIEPV YISQWGSMWI MMRREKRDRR H FKRMRFPP FDDEEPPLDY ADNILDVEPL EAIQLELDPE EDAPVLDWFY DHQPLRDSRK YVNGSTYQRW QFTLPMMSTL YR LANQLLT DLVDDNYFYL FDLKAFFTSK ALNMAIPGGP KFEPLVRDIN LQDEDWNEFN DINKIIIRQP IRTEYKIAFP YLY NNLPHH VHLTWYHTPN VVFIKTEDPD LPAFYFDPLI NPISHRHSVK SQEPLPDDDE EFELPEFVEP FLKDTPLYTD NTAN GIALL WAPRPFNLRS GRTRRALDIP LVKNWYREHC PAGQPVKVRV SYQKLLKYYV LNALKHRPPK AQKKRYLFRS FKATK FFQS TKLDWVEVGL QVCRQGYNML NLLIHRKNLN YLHLDYNFNL KPVKTLTTKE RKKSRFGNAF HLCREVLRLT KLVVDS HVQ YRLGNVDAFQ LADGLQYIFA HVGQLTGMYR YKYKLMRQIR MCKDLKHLIY YRFNTGPVGK GPGCGFWAAG WRVWLFF MR GITPLLERWL GNLLARQFEG RHSKGVAKTV TKQRVESHFD LELRAAVMHD ILDMMPEGIK QNKARTILQH LSEAWRCW K ANIPWKVPGL PTPIENMILR YVKAKADWWT NTAHYNRERI RRGATVDKTV CKKNLGRLTR LYLKAEQERQ HNYLKDGPY ITAEEAVAVY TTTVHWLESR RFSPIPFPPL SYKHDTKLLI LALERLKEAY SVKSRLNQSQ REELGLIEQA YDNPHEALSR IKRHLLTQR AFKEVGIEFM DLYSHLVPVY DVEPLEKITD AYLDQYLWYE ADKRRLFPPW IKPADTEPPP LLVYKWCQGI N NLQDVWET SEGECNVMLE SRFEKMYEKI DLTLLNRLLR LIVDHNIADY MTAKNNVVIN YKDMNHTNSY GIIRGLQFAS FI VQYYGLV MDLLVLGLHR ASEMAGPPQM PNDFLSFQDI ATEAAHPIRL FCRYIDRIHI FFRFTADEAR DLIQRYLTEH PDP NNENIV GYNNKKCWPR DARMRLMKHD VNLGRAVFWD IKNRLPRSVT TVQWENSFVS VYSKDNPNLL FNMCGFECRI LPKC RTSYE EFTHKDGVWN LQNEVTKERT AQCFLRVDDE SMQRFHNRVR QILMASGSTT FTKIVNKWNT ALIGLMTYFR EAVVN TQEL LDLLVKCENK IQTRIKIGLN SKMPSRFPPV VFYTPKELGG LGMLSMGHVL IPQSDLRWSK QTDVGITHFR SGMSHE EDQ LIPNLYRYIQ PWESEFIDSQ RVWAEYALKR QEAIAQNRRL TLEDLEDSWD RGIPRINTLF QKDRHTLAYD KGWRVRT DF KQYQVLKQNP FWWTHQRHDG KLWNLNNYRT DMIQALGGVE GILEHTLFKG TYFPTWEGLF WEKASGFEES MKWKKLTN A QRSGLNQIPN RRFTLWWSPT INRANVYVGF QVQLDLTGIF MHGKIPTLKI SLIQIFRAHL WQKIHESIVM DLCQVFDQE LDALEIETVQ KETIHPRKSY KMNSSCADIL LFASYKWNVS RPSLLADSKD VMDSTTTQKY WIDIQLRWGD YDSHDIERYA RAKFLDYTT DNMSIYPSPT GVLIAIDLAY NLHSAYGNWF PGSKPLIQQA MAKIMKANPA LYVLRERIRK GLQLYSSEPT E PYLSSQNY GELFSNQIIW FVDDTNVYRV TIHKTFEGNL TTKPINGAIF IFNPRTGQLF LKIIHTSVWA GQKRLGQLAK WK TAEEVAA LIRSLPVEEQ PKQIIVTRKG MLDPLEVHLL DFPNIVIKGS ELQLPFQACL KVEKFGDLIL KATEPQMVLF NLY DDWLKT ISSYTAFSRL ILILRALHVN NDRAKVILKP DKTTITEPHH IWPTLTDEEW IKVEVQLKDL ILADYGKKNN VNVA SLTQS EIRDIILGME ISAPSQQRQQ IAEIEKQTKE QSQLTATQTR TVNKHGDEII TSTTSNYETQ TFSSKTEWRV RAISA ANLH LRTNHIYVSS DDIKETGYTY ILPKNVLKKF ICISDLRAQI AGYLYGVSPP DNPQVKEIRC IVMVPQWGTH QTVHLP GQL PQHEYLKEME PLGWIHTQPN ESPQLSPQDV TTHAKIMADN PSWDGEKTII ITCSFTPGSC TLTAYKLTPS GYEWGRQ NT DKGNNPKGYL PSHYERVQML LSDRFLGFFM VPAQSSWNYN FMGVRHDPNM KYELQLANPK EFYHEVHRPS HFLNFALL Q EGEVYSADRE DLYA

UniProtKB: Pre-mRNA-processing-splicing factor 8

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Macromolecule #15: Pre-mRNA-splicing factor RBM22

MacromoleculeName: Pre-mRNA-splicing factor RBM22 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 46.959555 KDa
SequenceString: MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG VRMRFKKTEV CQTCSKLKNV CQTCLLDLE YGLPIQVRDA GLSFKDDMPK SDVNKEYYTQ NMEREISNSD GTRPVGMLGK ATSTSDMLLK LARTTPYYKR N RPHICSFW ...String:
MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG VRMRFKKTEV CQTCSKLKNV CQTCLLDLE YGLPIQVRDA GLSFKDDMPK SDVNKEYYTQ NMEREISNSD GTRPVGMLGK ATSTSDMLLK LARTTPYYKR N RPHICSFW VKGECKRGEE CPYRHEKPTD PDDPLADQNI KDRYYGINDP VADKLLKRAS TMPRLDPPED KTITTLYVGG LG DTITETD LRNHFYQFGE IRTITVVQRQ QCAFIQFATR QAAEVAAEKS FNKLIVNGRR LNVKWGRSQA ARGKEKEKDG TTD SGIKLE PVPGLPGALP PPPAAEEEAS ANYFNLPPSG PPAVVNIALP PPPGIAPPPP PGFGPHMFHP MGPPPPFMRA PGPI HYPSQ DPQRMGAHAG KHSSP

UniProtKB: Pre-mRNA-splicing factor RBM22

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Macromolecule #16: RING-type E3 ubiquitin-protein ligase PPIL2

MacromoleculeName: RING-type E3 ubiquitin-protein ligase PPIL2 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 58.910379 KDa
SequenceString: MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV FDLLNIVPWL KKYGTNPSNG EKLDGRSLI KLNFSKNSEG KYHCPVLFTV FTNNTHIVAV RTTGNVYAYE AVEQLNIKAK NFRDLLTDEP FSRQDIITLQ D PTNLDKFN ...String:
MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV FDLLNIVPWL KKYGTNPSNG EKLDGRSLI KLNFSKNSEG KYHCPVLFTV FTNNTHIVAV RTTGNVYAYE AVEQLNIKAK NFRDLLTDEP FSRQDIITLQ D PTNLDKFN VSNFYHVKNN MKIIDPDEEK AKQDPSYYLK NTNAETRETL QELYKEFKGD EILAATMKAP EKKKVDKLNA AH YSTGKVS ASFTSTAMVP ETTHEAAAID EDVLRYQFVK KKGYVRLHTN KGDLNLELHC DLTPKTCENF IRLCKKHYYD GTI FHRSIR NFVIQGGDPT GTGTGGESYW GKPFKDEFRP NLSHTGRGIL SMANSGPNSN RSQFFITFRS CAYLDKKHTI FGRV VGGFD VLTAMENVES DPKTDRPKEE IRIDATTVFV DPYEEADAQI AQERKTQLKV APETKVKSSQ PQAGSQGPQT FRQGV GKYI NPAATKRAAE EEPSTSATVP MSKKKPSRGF GDFSSW

UniProtKB: RING-type E3 ubiquitin-protein ligase PPIL2

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Macromolecule #17: SNW domain-containing protein 1

MacromoleculeName: SNW domain-containing protein 1 / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 60.326215 KDa
SequenceString: MALTSFLPAP TQLSQDQLEA EEKARSQRSR QTSLVSSRRE PPPYGYRKGW IPRLLEDFGD GGAFPEIHVA QYPLDMGRKK KMSNALAIQ VDSEGKIKYD AIARQGQSKD KVIYSKYTDL VPKEVMNADD PDLQRPDEEA IKEITEKTRV ALEKSVSQKV A AAMPVRAA ...String:
MALTSFLPAP TQLSQDQLEA EEKARSQRSR QTSLVSSRRE PPPYGYRKGW IPRLLEDFGD GGAFPEIHVA QYPLDMGRKK KMSNALAIQ VDSEGKIKYD AIARQGQSKD KVIYSKYTDL VPKEVMNADD PDLQRPDEEA IKEITEKTRV ALEKSVSQKV A AAMPVRAA DKLAPAQYIR YTPSQQGVAF NSGAKQRVIR MVEMQKDPME PPRFKINKKI PRGPPSPPAP VMHSPSRKMT VK EQQEWKI PPCISNWKNA KGYTIPLDKR LAADGRGLQT VHINENFAKL AEALYIADRK AREAVEMRAQ VERKMAQKEK EKH EEKLRE MAQKARERRA GIKTHVEKED GEARERDEIR HDRRKERQHD RNLSRAAPDK RSKLQRNENR DISEVIALGV PNPR TSNEV QYDQRLFNQS KGMDSGFAGG EDEIYNVYDQ AWRGGKDMAQ SIYRPSKNLD KDMYGDDLEA RIKTNRFVPD KEFSG SDRR QRGREGPVQF EEDPFGLDKF LEEAKQHGGS KRPSDSSRPK EH

UniProtKB: SNW domain-containing protein 1

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Macromolecule #18: INOSITOL HEXAKISPHOSPHATE

MacromoleculeName: INOSITOL HEXAKISPHOSPHATE / type: ligand / ID: 18 / Number of copies: 1 / Formula: IHP
Molecular weightTheoretical: 660.035 Da
Chemical component information

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE

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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: 7.9
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 39.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: ab initio
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.12 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 35015
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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