BMRB Entry 34803

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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/BMR34803
MolProbity Validation Chart

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Title:
Solution structure of 6xHIS-tagged wild-type Gaussia luciferase
Deposition date:
2023-04-12
Original release date:
2024-02-26
Authors:
Dijkema, F.; Teilum, K.; Prestel, A.; Winther, J.
Citation:

Citation: Dijkema, F.; Teilum, K.; Prestel, A.; Winther, J.. "The inactivation mechanism of Gaussia luciferase and the structural basis for its substrate cooperativity"  .

Assembly members:

Assembly members:
entity_1, polymer, 175 residues, 19155.137 Da.

Natural source:

Natural source:   Common Name: Gaussia princeps   Taxonomy ID: 148582   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gaussia princeps

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET-29b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHKPTENNEDFNIVA VASNFATTDLDADRGKLPGK KLPLEVLKEMEANARKAGCT RGCLICLSHIKCTPKMKKFI PGRCHTYEGDKESAQGGIGE AIVDIPEIPGFKDLEPMEQF IAQVDLCVDCTTGCLKGLAN VQCSDLLKKWLPQRCATFAS KIQGQVDKIKGAGGD

Data sets:
Data typeCount
13C chemical shifts772
15N chemical shifts188
1H chemical shifts1252

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 175 residues - 19155.137 Da.

1   METHISHISHISHISHISHISLYSPROTHR
2   GLUASNASNGLUASPPHEASNILEVALALA
3   VALALASERASNPHEALATHRTHRASPLEU
4   ASPALAASPARGGLYLYSLEUPROGLYLYS
5   LYSLEUPROLEUGLUVALLEULYSGLUMET
6   GLUALAASNALAARGLYSALAGLYCYSTHR
7   ARGGLYCYSLEUILECYSLEUSERHISILE
8   LYSCYSTHRPROLYSMETLYSLYSPHEILE
9   PROGLYARGCYSHISTHRTYRGLUGLYASP
10   LYSGLUSERALAGLNGLYGLYILEGLYGLU
11   ALAILEVALASPILEPROGLUILEPROGLY
12   PHELYSASPLEUGLUPROMETGLUGLNPHE
13   ILEALAGLNVALASPLEUCYSVALASPCYS
14   THRTHRGLYCYSLEULYSGLYLEUALAASN
15   VALGLNCYSSERASPLEULEULYSLYSTRP
16   LEUPROGLNARGCYSALATHRPHEALASER
17   LYSILEGLNGLYGLNVALASPLYSILELYS
18   GLYALAGLYGLYASP

Samples:

sample_2: Gaussia luciferase, [U-15N; U-13C], 0.8 mM; sodium azide 0.02 % w/v; sodium dihydrogen phosphate 50 mM; sodium trimethylsilylpropanesulfonate (DSS) 0.125 mM; sodium hydroxide 7.5 mM

sample_conditions_1: ionic strength: 57.6 mM; pH: 6.0; pressure: 1 atm; temperature: 308.15 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

X-PLOR NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement

CcpNmr Analysis v2.5, CcpNmr - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III HD 750 MHz

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