BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 36288

Title: Solution structure of Gaussia Liciferase by NMR

Deposition date: 2019-09-19 Original release date: 2019-11-20

Authors: Kobayashi, N.; Yamazaki, T.

Citation: Wu, N.; Kobayashi, N.; Tsuda, K.; Unzai, S.; Saotome, T.; Kuroda, Y.; Yamazaki, T.. "Solution structure of Gaussia Liciferase by NMR"  . ., .-..

Assembly members:
entity_1, polymer, 174 residues, 18851.838 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

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
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_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-100% 13C; U-100% 15N], 0.2 mM; MES 50 mM; sodium azide 2 mM; D2O, [U-2H], 10%; H2O 90%

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
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1anisotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure calculation

MAGRO v2.01.33, Kobayashi - data analysis

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

NMRView v9.0, Johnson, One Moon Scientific - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

TopSpin v3.5, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts