BMRB Entry 50985

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50985
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Title:
1H, 13C and 15N Chemical Shift Assignments of the R957C mutant from Arkadia (RNF111) E3 RING domain in solution
Deposition date:
2021-06-17
Original release date:
2022-03-19
Authors:
Marousis, Konstantinos; Birkou, Maria; Raptis, Vasilis; Chasapis, Christos; Episkopou, Vasso; Bentrop, Detlef; Spyroulias, Georgios
Citation:

Citation: Birkou, Maria; Raptis, Vasilios; Marousis, Konstantinos; Tsevis, Athanasios; Bourikas, Kyriakos; Bentrop, Detlef; Episkopou, Vasso; Spyroulias, Georgios. "Impact of a Single Nucleotide Polymorphism on the 3D Protein Structure and Ubiquitination Activity of E3 Ubiquitin Ligase Arkadia"  Front. Mol. Biosci. 9, 844129-844129 (2022).
PubMed: 35281275

Assembly members:

Assembly members:
entity_1, polymer, 69 residues, 7897 Da.
entity_ZN, non-polymer, 65.409 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: pGEX

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKQDGEEGTEEDTEEKCTIC LSILEEGEDVRCLPCMHLFH QVCVDQWLITNKKCPICRVD IEAQLPSES

Data sets:
Data typeCount
13C chemical shifts214
15N chemical shifts66
1H chemical shifts428

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1R957C1
2ZN12
3ZN22

Entities:

Entity 1, R957C 69 residues - 7897 Da.

1   METLYSGLNASPGLYGLUGLUGLYTHRGLU
2   GLUASPTHRGLUGLULYSCYSTHRILECYS
3   LEUSERILELEUGLUGLUGLYGLUASPVAL
4   ARGCYSLEUPROCYSMETHISLEUPHEHIS
5   GLNVALCYSVALASPGLNTRPLEUILETHR
6   ASNLYSLYSCYSPROILECYSARGVALASP
7   ILEGLUALAGLNLEUPROSERGLUSER

Entity 2, ZN1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: R957C, [U-99% 15N], 0.4 mM; DSS 0.25 mM; potassium phosphate 50 mM

sample_2: R957C, [U-98% 13C; U-98% 15N], 0.5 mM; DSS 0.25 mM; potassium phosphate 50 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HN(CO)CACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1

Software:

CARA v1.5.5 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Related Database Links:

UNP Q6ZNA4
AlphaFold Q9NSR1

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