BMRB Entry 34711

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34711
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution NMR structure of N-acetylglucosaminyltransferase V (GnTV) G26P mutant TMD
Deposition date:
2022-02-22
Original release date:
2023-01-02
Authors:
Silber, M.; Muhle-Goll, C.
Citation:

Citation: Papadopoulou, Alkmini; Stelzer, Walter; Silber, Mara; Schlosser, Christine; Spitz, Charlotte; Haug-Kroper, Martina; Straub, Tobias; Muller, Stephan; Lichtenthaler, Stefan; Muhle-Goll, Claudia; Langosch, Dieter; Fluhrer, Regina. "Helical stability of the GnTV transmembrane domain impacts on SPPL3 dependent cleavage"  Sci. Rep. 12, 20987-20987 (2022).
PubMed: 36470941

Assembly members:

Assembly members:
entity_1, polymer, 29 residues, 3591.487 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KKKLGFFLVTFGFIWPMMLL HFTIQQRKK

Data sets:
Data typeCount
13C chemical shifts105
15N chemical shifts28
1H chemical shifts212

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 29 residues - 3591.487 Da.

1   LYSLYSLYSLEUGLYPHEPHELEUVALTHR
2   PHEGLYPHEILETRPPROMETMETLEULEU
3   HISPHETHRILEGLNGLNARGLYSLYS

Samples:

sample_1: GNTV_G26P 0.5 mM

sample_conditions_1: ionic strength: 1 Not defined; pH: 7.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CcpNmr Analysis, Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, Llinas M, Ulrich EL, Markley JL, Ionides J, Laue ED - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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