BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30020

Title: The C-terminal domain of rice beta-galactosidase 1   PubMed: 27451952

Deposition date: 2016-02-22 Original release date: 2016-08-08

Authors: Rimlumduan, T.; Hua, Y.-l.; Tanaka, T.; Ketudat-Cairns, J.R.

Citation: Rimlumduan, T.; Hua, Y.-l.; Tanaka, T.; Ketudat-Cairns, J.R.. "Structure of a plant beta-galactosidase C-terminal domain"  Biochim. Biophys. Acta 1864, 1411-1418 (2016).

Assembly members:
entity_1, polymer, 122 residues, 13029.779 Da.

Natural source:   Common Name: Rice   Taxonomy ID: 39946   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Oryza sativa

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

Entity Sequences (FASTA):
entity_1: GSHMRTVSGVCADVSEYHPN IKNWQIESYGEPEFHTAKVH LKCAPGQTISAIKFASFGTP LGTCGTFQQGECHSINSNSV LERKCIGLERCVVAISPSNF GGDPCPEVMKRVAVEAVCST AA

Data sets:
Data typeCount
13C chemical shifts444
15N chemical shifts114
1H chemical shifts775

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 122 residues - 13029.779 Da.

1   GLYSERHISMETARGTHRVALSERGLYVAL
2   CYSALAASPVALSERGLUTYRHISPROASN
3   ILELYSASNTRPGLNILEGLUSERTYRGLY
4   GLUPROGLUPHEHISTHRALALYSVALHIS
5   LEULYSCYSALAPROGLYGLNTHRILESER
6   ALAILELYSPHEALASERPHEGLYTHRPRO
7   LEUGLYTHRCYSGLYTHRPHEGLNGLNGLY
8   GLUCYSHISSERILEASNSERASNSERVAL
9   LEUGLUARGLYSCYSILEGLYLEUGLUARG
10   CYSVALVALALAILESERPROSERASNPHE
11   GLYGLYASPPROCYSPROGLUVALMETLYS
12   ARGVALALAVALGLUALAVALCYSSERTHR
13   ALAALA

Samples:

sample_1: D2O, [U-2H], 5%; H2O 95%; OsBGal1 Cter 0.5 mM; sodium chloride 100 mM; sodium phosphate 20 mM

sample_2: D2O, [U-2H], 100%; OsBGal1 Cter 0.54 mM; sodium chloride 100 mM; sodium phosphate 20 mM

sample_3: D2O, [U-2H], 5%; H2O 95%; OsBGal1 Cter, [U-100% 15N], 0.79 mM; sodium chloride 100 mM; sodium phosphate 20 mM

sample_4: D2O, [U-2H], 5%; H2O 95%; OsBGal1 Cter, [U-100% 13C; U-100% 15N], 0.5 mM; sodium chloride 100 mM; sodium phosphate 20 mM

sample_5: D2O, [U-2H], 5%; H2O 95%; OsBGal1 Cter, [U-10% 13C], 0.18 mM; sodium chloride 100 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D HNHAsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_4isotropicsample_conditions_1
3D HNCACBsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D C(CO)NHsample_4isotropicsample_conditions_1
3D HBCBCACOCAHAsample_4isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1
2D 1H-13C HSQCsample_5isotropicsample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

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

PIPP, Garrett - peak picking

ProcheckNMR, Laskowski and MacArthur - data analysis

X-PLOR vv3.1, Brunger - structure calculation

NMR spectrometers:

  • Varian UNITY INOVA 500 MHz
  • Bruker AVANCE DRX 800 MHz
  • Bruker AVANCE III 800 MHz

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