BMRB Entry 51822

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51822

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Title:
Backbone assignment of MAGEA4-MHD in complex with RAD18-R6BD
Deposition date:
2023-02-05
Original release date:
2024-02-06
Authors:
Alvarez, Lucia; Hennig, Janosch; Simon, Bernd; Schweimer, Kristian; Griffith-Jones, Simonne; Bhogaraju, Sagar
Citation:

Citation: Griffith-Jones, Simonne; Alvarez, Lucia; Mukhopadhyay, Urbi; Gharbi, Sarah; Rettel, Mandy; Adams, Michael; Hennig, Janosch; Bhogaraju, Sagar. "Structural basis for RAD18 regulation by MAGEA4 and its implications for RING ubiquitin ligase binding by MAGE family proteins"  EMBO J. 43, 1273-1300 (2024).
PubMed: 38448672

Assembly members:

Assembly members:
entity_1, polymer, 236 residues, 26877.74 Da.
entity_2, polymer, 27 residues, 3207.77 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pCoofy1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKHHHHHHSAGLEVLFQGPD AESLFREALSNKVDELAHFL LRKYRAKELVTKAEMLERVI KNYKRCFPVIFGKASESLKM IFGIDVKEVDPTSNTYTLVT CLGLSYDGLLGNNQIFPKTG LLIIVLGTIAMEGDSASEEE IWEELGVMGVYDGREHTVYG EPRKLLTQDWVQENYLEYRQ VPGSNPARYEFLWGPRALAE TSYVKVLEHVVRVNARVRIA YPSLREAALLEEEEGV
entity_2: SKYRKKHKSEFQLLVDQARK GYKKIAG

Data sets:
Data typeCount
15N chemical shifts159
1H chemical shifts159

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MAGEA4-MHD1
2RAD182

Entities:

Entity 1, MAGEA4-MHD 236 residues - 26877.74 Da.

1   METLYSHISHISHISHISHISHISSERALA
2   GLYLEUGLUVALLEUPHEGLNGLYPROASP
3   ALAGLUSERLEUPHEARGGLUALALEUSER
4   ASNLYSVALASPGLULEUALAHISPHELEU
5   LEUARGLYSTYRARGALALYSGLULEUVAL
6   THRLYSALAGLUMETLEUGLUARGVALILE
7   LYSASNTYRLYSARGCYSPHEPROVALILE
8   PHEGLYLYSALASERGLUSERLEULYSMET
9   ILEPHEGLYILEASPVALLYSGLUVALASP
10   PROTHRSERASNTHRTYRTHRLEUVALTHR
11   CYSLEUGLYLEUSERTYRASPGLYLEULEU
12   GLYASNASNGLNILEPHEPROLYSTHRGLY
13   LEULEUILEILEVALLEUGLYTHRILEALA
14   METGLUGLYASPSERALASERGLUGLUGLU
15   ILETRPGLUGLULEUGLYVALMETGLYVAL
16   TYRASPGLYARGGLUHISTHRVALTYRGLY
17   GLUPROARGLYSLEULEUTHRGLNASPTRP
18   VALGLNGLUASNTYRLEUGLUTYRARGGLN
19   VALPROGLYSERASNPROALAARGTYRGLU
20   PHELEUTRPGLYPROARGALALEUALAGLU
21   THRSERTYRVALLYSVALLEUGLUHISVAL
22   VALARGVALASNALAARGVALARGILEALA
23   TYRPROSERLEUARGGLUALAALALEULEU
24   GLUGLUGLUGLUGLYVAL

Entity 2, RAD18 27 residues - 3207.77 Da.

1   SERLYSTYRARGLYSLYSHISLYSSERGLU
2   PHEGLNLEULEUVALASPGLNALAARGLYS
3   GLYTYRLYSLYSILEALAGLY

Samples:

sample_1: MAGEA4-MHD, [U-100% 13C; U-100% 15N; U-80% 2H], 105 uM; RAD18-R6BD 315 uM; NaCl 200 mM; HEPES 20 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CARA v1.9.1.7 - chemical shift assignment

NMRPipe - processing

NMR spectrometers:

  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE III 1000 MHz

Related Database Links:

UNP P43358

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks