BMRB Entry 36385

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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/BMR36385
MolProbity Validation Chart

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Title:
Solution structure of Gaussia Liciferase by NMR
Deposition date:
2020-09-17
Original release date:
2021-06-10
Authors:
Kobayashi, N.; Wu, N.; Kuroda, Y.; Yamazaki, T.
Citation:

Citation: Wu, N.; Kobayashi, N.; Tsuda, K.; Unzai, S.; Saotome, T.; Kuroda, Y.; Yamazaki, T.. "Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR."  Sci. Rep. 10, 20069-20069 (2020).
PubMed: 33208800

Assembly members:

Assembly members:
entity_1, polymer, 174 residues, 18851.838 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   Vector: pET21c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: TGKPTENNEDFNIVAVASNF ATTDLDADRGKLPGKKLPLE VLKEMEANARKAGCTRGCLI CLSHIKCTPKMKKFIPGRCH TYEGDKESAQGGIGEAIVDI PAIPRFKDLEPMEQFIAQVD LCVDCTTGCLKGLANVQCSD LLKKWLPQRCATFASKIQGQ VDKIKGAGGDIEGR

Data sets:
Data typeCount
13C chemical shifts689
15N chemical shifts177
1H chemical shifts1094

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 174 residues - 18851.838 Da.

1   THRGLYLYSPROTHRGLUASNASNGLUASP
2   PHEASNILEVALALAVALALASERASNPHE
3   ALATHRTHRASPLEUASPALAASPARGGLY
4   LYSLEUPROGLYLYSLYSLEUPROLEUGLU
5   VALLEULYSGLUMETGLUALAASNALAARG
6   LYSALAGLYCYSTHRARGGLYCYSLEUILE
7   CYSLEUSERHISILELYSCYSTHRPROLYS
8   METLYSLYSPHEILEPROGLYARGCYSHIS
9   THRTYRGLUGLYASPLYSGLUSERALAGLN
10   GLYGLYILEGLYGLUALAILEVALASPILE
11   PROALAILEPROARGPHELYSASPLEUGLU
12   PROMETGLUGLNPHEILEALAGLNVALASP
13   LEUCYSVALASPCYSTHRTHRGLYCYSLEU
14   LYSGLYLEUALAASNVALGLNCYSSERASP
15   LEULEULYSLYSTRPLEUPROGLNARGCYS
16   ALATHRPHEALASERLYSILEGLNGLYGLN
17   VALASPLYSILELYSGLYALAGLYGLYASP
18   ILEGLUGLYARG

Samples:

sample_1: Gluc, [U-13C; U-15N], 200 uM; MES 50 mM; sodium azide 2 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

MagRO-NMRView v2.01.33, Kobayashi, N. - chemical shift assignment, peak picking

NMRPipe v2017, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TopSpin v3.5, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

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