BMRB Entry 34997

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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/BMR34997
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Title:
Solution NMR structure of the lipoyl domain of the E2 subunit in the human alpha-ketoglutarate dehydrogenase complex
Deposition date:
2025-05-27
Original release date:
2026-06-05
Authors:
Czajlik, A.; Batta, G.; Ambrus, A.
Citation:

Citation: Czajlik, A.; Batta, G.; Ambrus, A.. "NMR Structural analysis of the lipoyl domain of the hKGDHc-E2 Protein"  .

Assembly members:

Assembly members:
entity_1, polymer, 84 residues, 8674.597 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 BL21(DE3)   Vector: PET52B+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGDDLVTVKTPAFAESVTE GDVRWEKAVGDTVAEDEVVC EIETDKTSVQVPSPANGVIE ALLVPDGGKVEGGTPLFTLR KTGA

Data sets:
Data typeCount
13C chemical shifts336
15N chemical shifts80
1H chemical shifts560

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 84 residues - 8674.597 Da.

1   GLYPROGLYASPASPLEUVALTHRVALLYS
2   THRPROALAPHEALAGLUSERVALTHRGLU
3   GLYASPVALARGTRPGLULYSALAVALGLY
4   ASPTHRVALALAGLUASPGLUVALVALCYS
5   GLUILEGLUTHRASPLYSTHRSERVALGLN
6   VALPROSERPROALAASNGLYVALILEGLU
7   ALALEULEUVALPROASPGLYGLYLYSVAL
8   GLUGLYGLYTHRPROLEUPHETHRLEUARG
9   LYSTHRGLYALA

Samples:

sample_1: Lipoyl domain of the E2 subunit in the human alpha-ketoglutarate dehydrogenase complex, [U-100% 13C; U-100% 15N], 7 mM; H2O 90%; D2O, [U-100% 2H], 10%; potassium phosphate 20 mM

sample_2: Lipoyl domain of the E2 subunit in the human alpha-ketoglutarate dehydrogenase complex, [U-100% 15N], 3 mM; H2O 90%; D2O, [U-100% 2H], 10%; potassium phosphate 20 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v3.8, Schwieters, Kuszewski, Tjandra and Clore - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNmr Analysis v2.5.2, CCPN - chemical shift assignment, peak picking

TopSpin v3.1, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AVANCE NEO 700 MHz

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