EMDB-10465: Structure of SWI/SNF chromatin remodeler RSC bound to a nucleosome

Basic information

• Entry: Database: EMDB / ID: EMD-10465
• Title: Structure of SWI/SNF chromatin remodeler RSC bound to a nucleosome
• Map data: verall density of RSC bound to the nucleosome.

Sample

• Complex: Chromatin remodelling complex RSC ('remodels the structure of chromatin') bound to a nucleosome
  • Complex: RSC core
    • Protein or peptide: x 13 types
  • Complex: ATPase domain of Sth1 bound to the nucleosome
    • Protein or peptide: x 4 types
  • Complex: DNA
    • DNA: x 2 types
• Ligand: x 1 types

• Keywords: Chromatin remodeler DNA binding Nucleosome binding ATPase Transcription / DNA BINDING PROTEIN

Function / homology

Function:

positive regulation of pseudohyphal growth by positive regulation of transcription from RNA polymerase II promoter / chromatin remodeling at centromere / RHO GTPases activate IQGAPs / RHO GTPases Activate WASPs and WAVEs / Regulation of actin dynamics for phagocytic cup formation / regulation of nuclear cell cycle DNA replication / Platelet degranulation / DNA translocase activity / : / nucleosome disassembly / RSC-type complex / SWI/SNF complex / ATP-dependent chromatin remodeler activity / NuA4 histone acetyltransferase complex / nuclear chromosome / rRNA transcription / chromosome, centromeric region / ATP-dependent activity, acting on DNA / cytoskeleton organization / meiotic cell cycle / helicase activity / chromosome segregation / transcription elongation by RNA polymerase II / positive regulation of transcription elongation by RNA polymerase II / transcription coregulator activity / base-excision repair / lysine-acetylated histone binding / chromatin DNA binding / double-strand break repair via nonhomologous end joining / structural constituent of chromatin / G2/M transition of mitotic cell cycle / double-strand break repair / nucleosome / chromatin organization / histone binding / DNA helicase / chromatin remodeling / protein heterodimerization activity / chromatin binding / chromatin / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / structural molecule activity / positive regulation of DNA-templated transcription / ATP hydrolysis activity / positive regulation of transcription by RNA polymerase II / DNA binding / zinc ion binding / nucleoplasm / ATP binding / nucleus

Domain/homology:

Rsc8/Ssr1/Ssr2, zinc finger, ZZ-type / Chromatin-remodelling complex, RSC SWI/SNF subunit Rsc7/Swp82 / Chromatin remodelling complex Rsc7/Swp82 subunit / DNA-binding RFX-type winged-helix domain / Transcription regulator protein Rtt102 / Rtt102p-like transcription regulator protein / RFX-type winged-helix DNA-binding domain profile. / Chromatin-remodeling complex component Sfh1/SNF5 / SMARCC, C-terminal / SWIRM-associated region 1 / SNF5/SMARCB1/INI1 / SNF5 / SMARCB1 / INI1 / Remodelling complex subunit Rsc/polybromo / Snf2, ATP coupling domain / Snf2-ATP coupling, chromatin remodelling complex / Snf2-ATP coupling, chromatin remodelling complex / HSA domain / Helicase/SANT-associated domain / HSA domain profile. / SWIRM domain / SWIRM domain / SWIRM domain profile. / SANT domain profile. / SWIB/MDM2 domain superfamily / SANT domain / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / Zinc-binding domain, present in Dystrophin, CREB-binding protein. / Zinc finger, ZZ type / Zinc finger, ZZ-type / Zinc finger, ZZ-type superfamily / Zinc finger ZZ-type profile. / Myb-like DNA-binding domain / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / Actin / Actin family / Actin / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site / Histone H2A signature. / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone H2A / Histone 2A / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Helicase conserved C-terminal domain / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Homeobox-like domain superfamily / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / ATPase, nucleotide binding domain / Histone-fold / Bromodomain, conserved site / Bromodomain signature. / helicase superfamily c-terminal domain / Bromodomain / Bromodomain profile. / bromo domain / Bromodomain / Bromodomain-like superfamily / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Winged helix-like DNA-binding domain superfamily / P-loop containing nucleoside triphosphate hydrolase

Component:

Histone H2B 1.1 / Histone H2A type 1 / Chromatin structure-remodeling complex protein RSC6 / Nuclear protein STH1/NPS1 / Chromatin structure-remodeling complex subunit RSC7 / Chromatin structure-remodeling complex protein RSC8 / Regulator of Ty1 transposition protein 102 / Histone H4 / Histone H3.2 / Chromatin structure-remodeling complex subunit RSC4 / Chromatin structure-remodeling complex subunit RSC9 / Actin-like protein ARP9 / Chromatin structure-remodeling complex subunit SFH1 / Chromatin structure-remodeling complex protein RSC58 / Actin-related protein 7 / Histone H2A / High temperature lethal protein 1

• Biological species: Saccharomyces cerevisiae S288C (yeast) / Xenopus laevis (African clawed frog) / synthetic construct (others) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Method: single particle reconstruction / cryo EM / Resolution: 15.0 Å
• Authors: Wagner FR / Dienemann C

Funding support

3 items

Organization	Grant number	Country
German Research Foundation (DFG)
European Research Council (ERC)
Volkswagen Foundation

• Citation: Journal: Nature / Year: 2020; Title: Structure of SWI/SNF chromatin remodeller RSC bound to a nucleosome.; Authors: Felix R Wagner / Christian Dienemann / Haibo Wang / Alexandra Stützer / Dimitry Tegunov / Henning Urlaub / Patrick Cramer / ; Abstract: Chromatin-remodelling complexes of the SWI/SNF family function in the formation of nucleosome-depleted, transcriptionally active promoter regions (NDRs). In the yeast Saccharomyces cerevisiae, the essential SWI/SNF complex RSC contains 16 subunits, including the ATP-dependent DNA translocase Sth1. RSC removes nucleosomes from promoter regions and positions the specialized +1 and -1 nucleosomes that flank NDRs. Here we present the cryo-electron microscopy structure of RSC in complex with a nucleosome substrate. The structure reveals that RSC forms five protein modules and suggests key features of the remodelling mechanism. The body module serves as a scaffold for the four flexible modules that we call DNA-interacting, ATPase, arm and actin-related protein (ARP) modules. The DNA-interacting module binds extra-nucleosomal DNA and is involved in the recognition of promoter DNA elements that influence RSC functionality. The ATPase and arm modules sandwich the nucleosome disc with the Snf2 ATP-coupling (SnAC) domain and the finger helix, respectively. The translocase motor of the ATPase module engages with the edge of the nucleosome at superhelical location +2. The mobile ARP module may modulate translocase-nucleosome interactions to regulate RSC activity. The RSC-nucleosome structure provides a basis for understanding NDR formation and the structure and function of human SWI/SNF complexes that are frequently mutated in cancer.

History

Deposition	Nov 8, 2019	-
Header (metadata) release	Dec 25, 2019	-
Map release	Mar 18, 2020	-
Update	Mar 27, 2024	-
Current status	Mar 27, 2024	Processing site: PDBe / Status: Released

Map

• File: Download / File: emd_10465.map.gz / Format: CCP4 / Size: 40.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
• Annotation: verall density of RSC bound to the nucleosome.
• Voxel size: X=Y=Z: 1.05 Å

Density

Contour Level	By AUTHOR: 0.0115 / Movie #1: 0.0115
Minimum - Maximum	-0.0050771316 - 0.04260584
Average (Standard dev.)	0.0008879349 (±0.0038265768)

• Symmetry: Space group: 1

Details

EMDB XML:

Map geometry	Axis order X Y Z Origin 0 0 0 Dimensions 340 340 340 Spacing 340 340 340
Cell	A=B=C: 356.99997 Å α=β=γ: 90.0 °

CCP4 map header:

mode	Image stored as Reals
Å/pix. X/Y/Z	1.05	1.05	1.05
M x/y/z	340	340	340
origin x/y/z	0.000	0.000	0.000
length x/y/z	357.000	357.000	357.000
α/β/γ	90.000	90.000	90.000
MAP C/R/S	1	2	3
start NC/NR/NS	0	0	0
NC/NR/NS	340	340	340
D min/max/mean	-0.005	0.043	0.001

Supplemental data

Mask #1

• File: emd_10465_msk_1.map

Mask #2

• File: emd_10465_msk_2.map

Mask #3

• File: emd_10465_msk_3.map

Mask #4

• File: emd_10465_msk_4.map

Mask #5

• File: emd_10465_msk_5.map

Mask #6

• File: emd_10465_msk_6.map

Additional map: Half-map 2 corresponding to map 8.

• File: emd_10465_additional_1.map
• Annotation: Half-map 2 corresponding to map 8.

Additional map: Half-map 2 corresponding to map 5.

• File: emd_10465_additional_10.map
• Annotation: Half-map 2 corresponding to map 5.

Additional map: Half-map 1 corresponding to map 5.

• File: emd_10465_additional_11.map
• Annotation: Half-map 1 corresponding to map 5.

Additional map: Map 5. Focused map of the body 1

• File: emd_10465_additional_12.map
• Annotation: Map 5. Focused map of the body 1

Additional map: Half-map 2 corresponding to map 4.

• File: emd_10465_additional_13.map
• Annotation: Half-map 2 corresponding to map 4.

Additional map: Half-map 1 corresponding to map 4.

• File: emd_10465_additional_14.map
• Annotation: Half-map 1 corresponding to map 4.

Additional map: Half-map 2 corresponding to map 3.

• File: emd_10465_additional_15.map
• Annotation: Half-map 2 corresponding to map 3.

Additional map: Half-map 1 corresponding to map 3.

• File: emd_10465_additional_16.map
• Annotation: Half-map 1 corresponding to map 3.

Additional map: Map 3. Focused map of the ATPase domain

• File: emd_10465_additional_17.map
• Annotation: Map 3. Focused map of the ATPase domain

Additional map: Half-map 2 corresponding to map 2.

• File: emd_10465_additional_18.map
• Annotation: Half-map 2 corresponding to map 2.

Additional map: Half-map 1 corresponding to map 2.

• File: emd_10465_additional_19.map
• Annotation: Half-map 1 corresponding to map 2.

Additional map: Half-map 1 corresponding to map 8.

• File: emd_10465_additional_2.map
• Annotation: Half-map 1 corresponding to map 8.

Additional map: Focused map of the nucleosome.

• File: emd_10465_additional_20.map
• Annotation: Focused map of the nucleosome.

Additional map: Map 4. Focused map of the arm module.

• File: emd_10465_additional_21.map
• Annotation: Map 4. Focused map of the arm module.

Additional map: Map 8. Composite map of the RSC

• File: emd_10465_additional_3.map
• Annotation: Map 8. Composite map of the RSC

Additional map: Half-map 2 corresponding to map 7.

• File: emd_10465_additional_4.map
• Annotation: Half-map 2 corresponding to map 7.

Additional map: Half-map 1 corresponding to map 7.

• File: emd_10465_additional_5.map
• Annotation: Half-map 1 corresponding to map 7.

Additional map: Map7. Composite map of the ATPase

• File: emd_10465_additional_6.map
• Annotation: Map7. Composite map of the ATPase

Additional map: Half-map 2 corresponding to map 6.

• File: emd_10465_additional_7.map
• Annotation: Half-map 2 corresponding to map 6.

Additional map: Half-map 1 corresponding to map 6.

• File: emd_10465_additional_8.map
• Annotation: Half-map 1 corresponding to map 6.

Additional map: Map 6. Focused map of the body 2

• File: emd_10465_additional_9.map
• Annotation: Map 6. Focused map of the body 2

Sample components

Entire : Chromatin remodelling complex RSC ('remodels the structure of chr...

• Entire: Name: Chromatin remodelling complex RSC ('remodels the structure of chromatin') bound to a nucleosome

Components

• Complex: Chromatin remodelling complex RSC ('remodels the structure of chromatin') bound to a nucleosome
  • Complex: RSC core
    • Protein or peptide: Chromatin structure-remodeling complex subunit SFH1
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC8
    • Protein or peptide: Chromatin structure-remodeling complex subunit RSC7
    • Protein or peptide: Chromatin structure-remodeling complex subunit RSC9
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC6
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC58
    • Protein or peptide: High temperature lethal protein 1
    • Protein or peptide: Chromatin structure-remodeling complex subunit RSC4
    • Protein or peptide: Nuclear protein STH1/NPS1
    • Protein or peptide: Actin-related protein 7
    • Protein or peptide: Actin-like protein ARP9
    • Protein or peptide: Regulator of Ty1 transposition protein 102
    • Protein or peptide: Unknown protein
  • Complex: ATPase domain of Sth1 bound to the nucleosome
    • Protein or peptide: Histone H3.2
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A
    • Protein or peptide: Histone H2B 1.1
  • Complex: DNA
    • DNA: DNA-I
    • DNA: DNA-J
• Ligand: ZINC ION

Supramolecule #1: Chromatin remodelling complex RSC ('remodels the structure of chr...

• Supramolecule: Name: Chromatin remodelling complex RSC ('remodels the structure of chromatin') bound to a nucleosome; type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#19

Supramolecule #2: RSC core

• Supramolecule: Name: RSC core / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #7-#19; Details: Composite map 8 made by Warp using the maps 4, 5, 6.
• Source (natural): Organism: Saccharomyces cerevisiae S288C (yeast)

Supramolecule #3: ATPase domain of Sth1 bound to the nucleosome

• Supramolecule: Name: ATPase domain of Sth1 bound to the nucleosome / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1-#4 / Details: Composite map 7 made by Warp using the maps 2, 3.
• Source (natural): Organism: Xenopus laevis (African clawed frog)

Supramolecule #4: DNA

• Supramolecule: Name: DNA / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #5-#6
• Source (natural): Organism: synthetic construct (others)

Macromolecule #1: Histone H3.2

• Macromolecule: Name: Histone H3.2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Xenopus laevis (African clawed frog)
• Molecular weight: Theoretical: 15.30393 KDa
• Recombinant expression: Organism: Escherichia coli (E. coli)

Sequence

String:

ARTKQTARKS TGGKAPRKQL ATKAARKSAP ATGGVKKPHR YRPGTVALRE IRRYQKSTEL LIRKLPFQRL VREIAQDFKT DLRFQSSAV MALQEASEAY LVALFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA

UniProtKB: Histone H3.2

Macromolecule #2: Histone H4

• Macromolecule: Name: Histone H4 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Xenopus laevis (African clawed frog)
• Molecular weight: Theoretical: 11.263231 KDa
• Recombinant expression: Organism: Escherichia coli (E. coli)

Sequence

String:

SGRGKGGKGL GKGGAKRHRK VLRDNIQGIT KPAIRRLARR GGVKRISGLI YEETRGVLKV FLENVIRDAV TYTEHAKRKT VTAMDVVYA LKRQGRTLYG FGG

UniProtKB: Histone H4

Macromolecule #3: Histone H2A

• Macromolecule: Name: Histone H2A / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Xenopus laevis (African clawed frog)
• Molecular weight: Theoretical: 13.978241 KDa
• Recombinant expression: Organism: Escherichia coli (E. coli)

Sequence

String:

SGRGKQGGKT RAKAKTRSSR AGLQFPVGRV HRLLRKGNYA ERVGAGAPVY LAAVLEYLTA EILELAGNAA RDNKKTRIIP RHLQLAVRN DEELNKLLGR VTIAQGGVLP NIQSVLLPKK TESSKSAKSK

UniProtKB: Histone H2A

Macromolecule #4: Histone H2B 1.1

• Macromolecule: Name: Histone H2B 1.1 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Xenopus laevis (African clawed frog)
• Molecular weight: Theoretical: 13.524752 KDa
• Recombinant expression: Organism: Escherichia coli (E. coli)

Sequence

String:

AKSAPAPKKG SKKAVTKTQK KDGKKRRKTR KESYAIYVYK VLKQVHPDTG ISSKAMSIMN SFVNDVFERI AGEASRLAHY NKRSTITSR EIQTAVRLLL PGELAKHAVS EGTKAVTKYT SAK

UniProtKB: Histone H2B 1.1

Macromolecule #7: Chromatin structure-remodeling complex subunit SFH1

• Macromolecule: Name: Chromatin structure-remodeling complex subunit SFH1 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 48.83318 KDa

Sequence

String:

MSHQNQLIPQ AYISNFHNRL TNEDDGIPIF TMAQQTRQHK RAKVVNYAEY DNDLFDEFNM NGSNFNNADT HYKDNAVSHE NTPALTNGV TMDGSEYNVL ENMNGADSII SNNKYDAGSN MVVESLSGLN SNNNASNGPS NKAQAQDIGN AVLPDLQDQH H NPFNILRY PKIRDTFING KVVSPYRLNT DQETKANANS GEAIMIPITL DIEHMGHTIK DQFLWNYNDD SISPEEFASI YC KDLDMTS ATLQTQIANI IKEQLKDLEN IAATEIMSDL HVIINLTCNL QDRFFEDNFQ WNLNDKSLTP ERFATSIVQD LGL TREFIP LISQSLHETI LKIKKDWVDG HLIQDHVPND AAFGYLSGIR LDIDELGSNW CPRVEILTKE EIQKREIEKE RNLR RLKRE TDRLSRRGRR RLDDLETTMR M

UniProtKB: Chromatin structure-remodeling complex subunit SFH1

Macromolecule #8: Chromatin structure-remodeling complex protein RSC8

• Macromolecule: Name: Chromatin structure-remodeling complex protein RSC8 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 126.489883 KDa

Sequence

String:

MSDTEKDKDV PMVDSHEATE EPPTTSTNTP SFPHLAQEQA KEESATLGAE VAHKKINYEQ EAQKLEEKAL RFLAKQTHPV IIPSFASWF DISKIHEIEK RSNPDFFNDS SRFKTPKAYK DTRNFIINTY RLSPYEYLTI TAVRRNVAMD VASIVKIHAF L EKWGLINY QIDPRTKPSL IGPSFTGHFQ VVLDTPQGLK PFLPENVIKQ EVEGGDGAEP QVKKEFPVNL TIKKNVYDSA QD FNALQDE SRNSRQIHKV YICHTCGNES INVRYHNLRA RDTNLCSRCF QEGHFGANFQ SSDFIRLENN GNSVKKNWSD QEM LLLLEG IEMYEDQWEK IADHVGGHKR VEDCIEKFLS LPIEDNYIRE VVGSTLNGKG GDSRDGSVSG SKLMECVNDA VQTL LQGDD KLGKVSDKSR EISEKYIEES QAIIQELVKL TMEKLESKFT KLCDLETQLE MEKLKYVKES EKMLNDRLSL SKQIL DLNK SLEELNVSKK LVLISEQVDS GIQLVEKDQE GDDEDGNTAT GHGVKRVGKE GEEVGEGDSI AKLQPQVYKP WSLMSD TEK DKDVPMVDSH EATEEPPTTS TNTPSFPHLA QEQAKEESAT LGAEVAHKKI NYEQEAQKLE EKALRFLAKQ THPVIIP SF ASWFDISKIH EIEKRSNPDF FNDSSRFKTP KAYKDTRNFI INTYRLSPYE YLTITAVRRN VAMDVASIVK IHAFLEKW G LINYQIDPRT KPSLIGPSFT GHFQVVLDTP QGLKPFLPEN VIKQEVEGGD GAEPQVKKEF PVNLTIKKNV YDSAQDFNA LQDESRNSRQ IHKVYICHTC GNESINVRYH NLRARDTNLC SRCFQEGHFG ANFQSSDFIR LENNGNSVKK NWSDQEMLLL LEGIEMYED QWEKIADHVG GHKRVEDCIE KFLSLPIEDN YIREVVGSTL NGKGGDSRDG SVSGSKLMEC VNDAVQTLLQ G DDKLGKVS DKSREISEKY IEESQAIIQE LVKLTMEKLE SKFTKLCDLE TQLEMEKLKY VKESEKMLND RLSLSKQILD LN KSLEELN VSKKLVLISE QVDSGIQLVE KDQEGDDEDG NTATGHGVKR VGKEGEEVGE GDSIAKLQPQ VYKPWSL

UniProtKB: Chromatin structure-remodeling complex protein RSC8

Macromolecule #9: Chromatin structure-remodeling complex subunit RSC7

• Macromolecule: Name: Chromatin structure-remodeling complex subunit RSC7 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 49.71652 KDa

Sequence

String:

MSDSEGGLAS EVEHEKRSRS TSNRPNYAID TEDLDIDEND ENEDDDYREE EANEGVNEEE ISDEEEQINK SGRNKRRHVD EEEDLSEDK GVTRSRNRSK FKKPVFPGID DAEENLNPLK VVNEEYVLPD DPEGETKITA DGDLLGGREF LVRTFTLTEK G NRKFMLAT EPARIVGFRD SYLFFQTHPN LYKFILNQTQ KNDLIDRGVL PYSYRNRQIA LVTARGVFKE FGAKIIRGGK HI TDDYYAS ELRTKGNVIE GKLAGDPIDK SARALETMMY PASENGINPA KNQVEFFEHR PHGHMSNSNI IASGSKLSST NWL YQHSAA CSRFNSDLFY DRVKVLLVDQ QGLRDAYTNI LHIPESTQST TVLGWRRSKN DSPSDTSIVY ETVIHDNDLN KPKT GLSEI PKEIYEDVVD EDVLRAITEQ QNFEKCNEYI

UniProtKB: Chromatin structure-remodeling complex subunit RSC7

Macromolecule #10: Chromatin structure-remodeling complex subunit RSC9

• Macromolecule: Name: Chromatin structure-remodeling complex subunit RSC9 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 65.289309 KDa

Sequence

String:

MNSLASNTPL NGTPVSEAPA TSSEPVNMFE TMVANPIKVS RLQSNGVLTG PAANTKSIHY SLANFNVFQS LPKETARGVD DLTRMEMAL LSGIPEEIKW SLKKYLTYSN KAPYMISLRT LPDLLPLFKT FILPLERIVE GLNKSSICDS KAMDSLQMGL N ALLILRNL AQDTDSVQIL VKDREIKSFI LFILKKFQCV ATGDNKWQLY EGNATFFNEL THYTLDLMEA ISSYIAPAMK DD HYFQTLV SILNYTKDRY MVISILRSLS RLLVRSKANE ESAADNLDHK TLSLIVSFLL LECDSELIIA SLDFLYQYIL PGS QRITEL FKSKECSLIL EATLPNLLSY NIATPDYHLL QKHKIRLIKR LKPPAPKEPP NLSEDLFQQL FKLNEPLRST AWLR CCFEP VQEAEFTQIS LWRSYESKFG QPVRESGRKL LPAVEFIKNV SNAFNNAAAI VITDPVTGKK RFVIKGIQPR FKALG IADG ERESQVPISA LKSKFLNDSK EITPARQNSI PEVKFPQELS DVSKVACTFL CLLSNDTDDG AGSAFCQRIR PLVLHK LAD IPPLTLALSE YMENTSGL

UniProtKB: Chromatin structure-remodeling complex subunit RSC9

Macromolecule #11: Chromatin structure-remodeling complex protein RSC6

• Macromolecule: Name: Chromatin structure-remodeling complex protein RSC6 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 54.222691 KDa

Sequence

String:

MVTQTNPVPV TYPTDAYIPT YLPDDKVSNL ADLKKLIEMD SRLDLYLTRR RLDTSINLPT NTKTKDHPPN KEMLRIYVYN TTESSPRSD SGTPADSGKT TWTLRIEGKL LHESANGKHP FSEFLEGVAV DFKRLKPLGM GKKRKRDSSL SLPLNLQQPE Y NDQDSTMG DNDNGEDEDS AEAESREEIV DALEWNYDEN NVVEFDGIDI KRQGKDNLRC SITIQLRGVD GGKVQYSPNL AT LIGMQTG SVNDAVYSIY KYILINNLFV TEQTEAQDGS NDAEDSSNEN NNKNGAGDDD GVEGSTPKDK PELGEVKLDS LLQ KVLDTN AAHLPLMNVV QTVNKLVSPL PPIILDYTID LSKDTTYGAT TLDVDVSHIL HQPQPQPNLQ KEEETDAEDT AKLR EITKL ALQLNSSAQK YQFFHELSLH PRETLTHYLW SSKQNELVLQ GDQYFNEDAA RTSDIYSNNN NDRSLMGNIS LLYSQ GRL

UniProtKB: Chromatin structure-remodeling complex protein RSC6

Macromolecule #12: Chromatin structure-remodeling complex protein RSC58

• Macromolecule: Name: Chromatin structure-remodeling complex protein RSC58 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 57.871309 KDa

Sequence

String:

MTESVGGNKL VDFLVNVQSI LNAASVKCHV VDESFPAKFF EKNPDKIYES YCKFIKNRSN SEGLIRNEDK LVLTTINKRF ENGEYEPIQ GGFYKLYHDI KLVCTILIHF YPQGTRNYQL VDKFYKFSSE LLLRECCRIG IALTQTNNIK SRSGKLLSGN E MDEYDDDD ATELDKIISY DFIKISMNYT VPISQTYQIR TKDMDLFSSI ISKSNLDKRP HELPNTNFKI NNVLPQTDIE NE APRLGFV GANTSNIPDP TLPPTEMMTR FLHPNWYALP TTVWLKYGNY NSWAPSFNEN GTVVDSTTRG LIWLERIGYM DLY EKNEKK VKQEELLNTN EEGINRKQND ENNKNVDGKS NGVQDDGGDN DNDATIASAN SESTENKEQF IIKLQNLYNW TPSN YIGDD EIENFRNGTP DKLVSDSLLK LKRLRKERIL NKVLKPTTEE RELYFKVKRI LKEVILAKKV SKVPINNVRA FPVLQ TNYN GSIPVVRAQP GRKRKHKK

UniProtKB: Chromatin structure-remodeling complex protein RSC58

Macromolecule #13: High temperature lethal protein 1

• Macromolecule: Name: High temperature lethal protein 1 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 9.192524 KDa

Sequence

String:

MSQNNTISSM NPERAYNNVT LKNLTAFQLL SQRENICELL NLVESTERHN SIINPERQRM SLEEMKKMLD ALKNERKK

UniProtKB: High temperature lethal protein 1

Macromolecule #14: Chromatin structure-remodeling complex subunit RSC4

• Macromolecule: Name: Chromatin structure-remodeling complex subunit RSC4 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 72.372375 KDa

Sequence

String:

MVVKKRKLAT EAGGSDERPK YLPGKHPKNQ EKTPHVDYNA PLNPKSELFL DDWHIPKFNR FISFTLDVLI DKYKDIFKDF IKLPSRKFH PQYYYKIQQP MSINEIKSRD YEYEDGPSNF LLDVELLTKN CQAYNEYDSL IVKNSMQVVM LIEFEVLKAK N LKRNYLIN SEVKAKLLHY LNKLVDATEK KINQALLGAS SPKNLDDKVK LSEPFMELVD KDELPEYYEI VHSPMALSIV KQ NLEIGQY SKIYDFIIDM LLVFQNAHIF NDPSALIYKD ATTLTNYFNY LIQKEFFPEL QDLNERGEIN LEFDKFEFEN YLA IGGGGP AAAGALAISA LDNDIEPESN REDLIDQADY DFNHFEGLGN GYNRSLLTED YLLNPNNFKK LIAKPETVQS EVKN ERSTT SDIEKTNSLE SEHLKIPKYN VIKSMQKEMQ SLSEQHTMEY KPYKLIQQIY IFSSKNLYSQ ATKPLLGSRP SCNQN WVEY IFNGNELSQN ENAFSFMLQP MQTFLTLQSH LTSSLKDTET LLTINKEPVK SRTSNVNSNL SQPQQQENDV IGNDTK QDI ENLTIGGGNN NDIVGNDNDK RNNITEIFDI RLSEGLNHLM FRCEDKISHE TEFMNFWINV LP

UniProtKB: Chromatin structure-remodeling complex subunit RSC4

Macromolecule #15: Nuclear protein STH1/NPS1

• Macromolecule: Name: Nuclear protein STH1/NPS1 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA helicase
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 156.982406 KDa

Sequence

String:

MLQEQSELMS TVMNNTPTTV AALAAVAAAS ETNGKLGSEE QPEITIPKPR SSAQLEQLLY RYRAIQNHPK ENKLEIKAIE DTFRNISRD QDIYETKLDT LRKSIDKGFQ YDEDLLNKHL VALQLLEKDT DVPDYFLDLP DTKNDNTTAI EVDYSEKKPI K ISADFNAK AKSLGLESKF SNATKTALGD PDTEIRISAR ISNRINELER LPANLGTYSL DDCLEFITKD DLSSRMDTFK IK ALVELKS LKLLTKQKSI RQKLINNVAS QAHHNIPYLR DSPFTAAAQR SVQIRSKVIV PQTVRLAEEL ERQQLLEKRK KER NLHLQK INSIIDFIKE RQSEQWSRQE RCFQFGRLGA SLHNQMEKDE QKRIERTAKQ RLAALKSNDE EAYLKLLDQT KDTR ITQLL RQTNSFLDSL SEAVRAQQNE AKILHGEEVQ PITDEEREKT DYYEVAHRIK EKIDKQPSIL VGGTLKEYQL RGLEW MVSL YNNHLNGILA DEMGLGKTIQ SISLITYLYE VKKDIGPFLV IVPLSTITNW TLEFEKWAPS LNTIIYKGTP NQRHSL QHQ IRVGNFDVLL TTYEYIIKDK SLLSKHDWAH MIIDEGHRMK NAQSKLSFTI SHYYRTRNRL ILTGTPLQNN LPELWAL LN FVLPKIFNSA KTFEDWFNTP FANTGTQEKL ELTEEETLLI IRRLHKVLRP FLLRRLKKEV EKDLPDKVEK VIKCKLSG L QQQLYQQMLK HNALFVGAGT EGATKGGIKG LNNKIMQLRK ICNHPFVFDE VEGVVNPSRG NSDLLFRVAG KFELLDRVL PKFKASGHRV LMFFQMTQVM DIMEDFLRMK DLKYMRLDGS TKTEERTEML NAFNAPDSDY FCFLLSTRAG GLGLNLQTAD TVIIFDTDW NPHQDLQAQD RAHRIGQKNE VRILRLITTD SVEEVILERA MQKLDIDGKV IQAGKFDNKS TAEEQEAFLR R LIESETNR DDDDKAELDD DELNDTLARS ADEKILFDKI DKERMNQERA DAKAQGLRVP PPRLIQLDEL PKVFREDIEE HF KKEDSEP LGRIRQKKRV YYDDGLTEEQ FLEAVEDDNM SLEDAIKKRR EARERRRLRQ NGTKENEIET LENTPEASET SLI ENNSFT AAVDEETNAD KETTASRSKR RSSRKKRTIS IVTAEDKENT QEESTSQENG GAKVEEEVKS SSVEIINGSE SKKK KPKLT VKIKLNKTTV LENNDGKRAE EKPESKSPAK KTAAKKTKTK SKSLGIFPTV EKLVEEMREQ LDEVDSHPRT SIFEK LPSK RDYPDYFKVI EKPMAIDIIL KNCKNGTYKT LEEVRQALQT MFENARFYNE EGSWVYVDAD KLNEFTDEWF KEHSS

UniProtKB: Nuclear protein STH1/NPS1

Macromolecule #16: Actin-related protein 7

• Macromolecule: Name: Actin-related protein 7 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 54.613332 KDa

Sequence

String:

(MSE)TLNRKCVVI HNGSHRTVAG FSNVELPQCI IPSSYIKRTD EGGEAEFIFG TYN(MSE)IDAAAE KRNGDEVYTL VD SQGLPYN WDALE(MSE)QWRY LYDTQLKVSP EELPLVIT(MSE)P ATNGKPD(MSE)AI LERYYELAFD KLNVPVFQIV I EPLAIALS (MSE)GKSSAFVID IGASGCNVTP IIDGIVVKNA VVRSKFGGDF LDFQVHERLA PLIKEEND(MSE)E N (MSE)ADEQKRS TDVWYEASTW IQQFKST(MSE)LQ VSEKDLFELE RYYKEQADIY AKQQEQLKQ(MSE) DQQLQYTALT GSPNNPLVQ KKNFLFKPLN KTLTLDLKEC YQFAEYLFKP QLISDKFSPE DGLGPL(MSE)AKS VKKAGASINS (MSE)KA NTSTNP NGLGTSHINT NVGDNNSTAS SSNISPEQVY SLLLTNVIIT GSTSLIEG(MSE)E QRIIKELSIR FPQYKLTTFA NQV(MSE)(MSE)DRKI QGWLGALT(MSE)A NLPSWSLGKW YSKEDYETLK RDRKQSQATN ATN

UniProtKB: Actin-related protein 7

Macromolecule #17: Actin-like protein ARP9

• Macromolecule: Name: Actin-like protein ARP9 / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 53.366398 KDa

Sequence

String:

(MSE)APFRQDSIL IIYPRSQTTL VQFGLNEETF TVPELEIPTQ IYRTTRQDGS YTYHSTNKDN KAELIKPIQN GEIIDI SAF TQFLRLIFVS ILSDRANKNQ DAFEAELSNI PLLLITHHSW SQSDLEIITQ YVFESLEINN LIQLPASLAA TYS (MSE)ISLQN CCIIDVGTHH TDIIPIVDYA QLDHLVSSIP (MSE)GGQSINDSL KKLLPQWDDD QIESLKKSPI FEVLSD DAK KLSSFDFGNE NEDEDEGTLN VAEIITSGRD TREVLEERER GQKVKNVKNS DLEFNTFWDE KGNEIKVGKQ RFQGCNN LI KNISNRVGLT LDNIDDINKA KAVWENIIIV GGTTSISGFK EALLGQLLKD HLIIEPEEEK SKREEEAKSV LPAATKKK S KF(MSE)TNSTAFV PTIEYVQCPT VIKLAKYPDY FPEWKKSGYS EIIFLGAQIV SKQIFTHPKD TFYITREKYN (MSE) KGPAALWD VQF

UniProtKB: Actin-like protein ARP9

Macromolecule #18: Regulator of Ty1 transposition protein 102

• Macromolecule: Name: Regulator of Ty1 transposition protein 102 / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• Molecular weight: Theoretical: 18.005195 KDa

Sequence

String:

(MSE)DPQTLITKA NKVSYYGNPT SKESWRYDWY QPSKVSSNVQ QPQQQLGD(MSE)E NNLEKYPFRY KTWLRNQEDE KN LQRESCE DILDLKEFDR RILKKSL(MSE)TS HTKGDTSKAT GAPSANQGDE ALSVDDIRGA VGNSEAIPGL SAGVNNDNT KESKDVK(MSE)N

UniProtKB: Regulator of Ty1 transposition protein 102

Macromolecule #19: Unknown protein

• Macromolecule: Name: Unknown protein / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Saccharomyces cerevisiae S288C (yeast)
• Molecular weight: Theoretical: 32.613104 KDa

Sequence

String:

(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

Macromolecule #5: DNA-I

• Macromolecule: Name: DNA-I / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA
• Source (natural): Organism: synthetic construct (others)
• Molecular weight: Theoretical: 72.876344 KDa

Sequence

String:

(DC)(DC)(DT)(DA)(DC)(DG)(DG)(DA)(DC)(DC) (DG)(DG)(DA)(DT)(DA)(DT)(DC)(DT)(DT)(DC) (DC)(DC)(DT)(DG)(DT)(DG)(DT)(DA)(DT) (DG)(DG)(DG)(DT)(DT)(DT)(DC)(DC)(DA)(DT) (DC) (DA)(DG)(DA)(DA)(DT)(DC)(DC)(DC) (DG)(DG)(DT)(DG)(DC)(DC)(DG)(DA)(DG)(DG) (DC)(DC) (DG)(DC)(DT)(DC)(DA)(DA)(DT) (DT)(DG)(DG)(DT)(DC)(DG)(DT)(DA)(DG)(DA) (DC)(DA)(DG) (DC)(DT)(DC)(DT)(DA)(DG) (DC)(DA)(DC)(DC)(DG)(DC)(DT)(DT)(DA)(DA) (DA)(DC)(DG)(DC) (DA)(DC)(DG)(DT)(DA) (DC)(DG)(DC)(DG)(DC)(DT)(DG)(DT)(DC)(DC) (DC)(DC)(DC)(DG)(DC) (DG)(DT)(DT)(DT) (DT)(DA)(DA)(DC)(DC)(DG)(DC)(DC)(DA)(DA) (DG)(DG)(DG)(DG)(DA)(DT) (DT)(DA)(DC) (DT)(DC)(DC)(DC)(DT)(DA)(DG)(DT)(DC)(DT) (DC)(DC)(DA)(DG)(DG)(DC)(DA) (DC)(DG) (DT)(DG)(DT)(DC)(DA)(DG)(DA)(DT)(DA)(DT) (DA)(DT)(DA)(DC)(DA)(DT)(DC)(DG) (DA) (DT)(DT)(DT)(DA)(DA)(DC)(DT)(DC)(DT)(DT) (DT)(DT)(DC)(DG)(DT)(DC)(DG)(DG)(DT) (DT)(DT)(DT)(DT)(DT)(DT)(DC)(DG)(DC)(DC) (DT)(DT)(DT)(DA)(DA)(DA)(DA)(DC)(DT)(DA) (DG)(DG)(DC)(DG)(DG)(DG)(DC)(DT)(DG) (DG)(DG)(DT)(DA)(DA)(DT)(DG)(DA)

Macromolecule #6: DNA-J

• Macromolecule: Name: DNA-J / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA
• Source (natural): Organism: synthetic construct (others)
• Molecular weight: Theoretical: 73.478852 KDa

Sequence

String:

(DT)(DC)(DA)(DT)(DT)(DA)(DC)(DC)(DC)(DA) (DG)(DC)(DC)(DC)(DG)(DC)(DC)(DT)(DA)(DG) (DT)(DT)(DT)(DT)(DA)(DA)(DA)(DG)(DG) (DC)(DG)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DC) (DC) (DG)(DA)(DC)(DG)(DA)(DA)(DA)(DA) (DG)(DA)(DG)(DT)(DT)(DA)(DA)(DA)(DT)(DC) (DG)(DA) (DT)(DG)(DT)(DA)(DT)(DA)(DT) (DA)(DT)(DC)(DT)(DG)(DA)(DC)(DA)(DC)(DG) (DT)(DG)(DC) (DC)(DT)(DG)(DG)(DA)(DG) (DA)(DC)(DT)(DA)(DG)(DG)(DG)(DA)(DG)(DT) (DA)(DA)(DT)(DC) (DC)(DC)(DC)(DT)(DT) (DG)(DG)(DC)(DG)(DG)(DT)(DT)(DA)(DA)(DA) (DA)(DC)(DG)(DC)(DG) (DG)(DG)(DG)(DG) (DA)(DC)(DA)(DG)(DC)(DG)(DC)(DG)(DT)(DA) (DC)(DG)(DT)(DG)(DC)(DG) (DT)(DT)(DT) (DA)(DA)(DG)(DC)(DG)(DG)(DT)(DG)(DC)(DT) (DA)(DG)(DA)(DG)(DC)(DT)(DG) (DT)(DC) (DT)(DA)(DC)(DG)(DA)(DC)(DC)(DA)(DA)(DT) (DT)(DG)(DA)(DG)(DC)(DG)(DG)(DC) (DC) (DT)(DC)(DG)(DG)(DC)(DA)(DC)(DC)(DG)(DG) (DG)(DA)(DT)(DT)(DC)(DT)(DG)(DA)(DT) (DG)(DG)(DA)(DA)(DA)(DC)(DC)(DC)(DA)(DT) (DA)(DC)(DA)(DC)(DA)(DG)(DG)(DG)(DA)(DA) (DG)(DA)(DT)(DA)(DT)(DC)(DC)(DG)(DG) (DT)(DC)(DC)(DG)(DT)(DA)(DG)(DG)

Macromolecule #20: ZINC ION

• Macromolecule: Name: ZINC ION / type: ligand / ID: 20 / Number of copies: 1 / Formula: ZN
• Molecular weight: Theoretical: 65.409 Da

Experimental details

Structure determination

• Method: cryo EM
• Processing: single particle reconstruction
• Aggregation state: particle

Sample preparation

• Buffer: pH: 7.6
• Vitrification: Cryogen name: ETHANE

Electron microscopy

• Microscope: FEI TITAN KRIOS
• Electron beam: Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
• Electron optics: Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
• Image recording: Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 45.4 e/Ų
• Experimental equipment: Model: Titan Krios / Image courtesy: FEI Company

Image processing

• Startup model: Type of model: INSILICO MODEL / Details: CryoSPARC
• Initial angle assignment: Type: COMMON LINE / Details: CryoSPARC
• Final angle assignment: Type: MAXIMUM LIKELIHOOD / Details: RELION
• Final reconstruction: Resolution.type: BY AUTHOR / Resolution: 15.0 Å / Resolution method: OTHER / Number images used: 372442