BMRB Entry 25951

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25951

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Title:
1H, 13C, and 15N chemical shift assignments of the fucose-bound lectin from Ralstonia solanacearum
Deposition date:
2016-01-12
Original release date:
2016-02-18
Authors:
Antonik, Pawel; van Nuland, Nico; Volkov, Alexander; Crowley, Peter
Citation:

Citation: Antonik, Pawel; Volkov, Alexander; Broder, Ursula; Re, Daniele; van Nuland, Nico; Crowley, Peter. "Anomer-Specific Recognition and Dynamics in a Fucose-Binding Lectin"  Biochemistry 55, 1195-1203 (2016).
PubMed: 26845253

Assembly members:

Assembly members:
RSL, polymer, 90 residues, Formula weight is not available
ALPHA-L-FUCOSE, non-polymer, 164.156 Da.

Natural source:

Natural source:   Common Name: b-proteobacteria   Taxonomy ID: 305   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Ralstonia solanacearum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RSL: SSVQTAATSWGTVPSIRVYT ANNGKITERCWDGKGWYTGA FNEPGDNVSVTSWLVGSAIH IRVYASTGTTTTEWCWDGNG WTKGAYTATN

Data sets:
Data typeCount
13C chemical shifts510
15N chemical shifts192
1H chemical shifts220

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RSL1
2ligand2

Entities:

Entity 1, RSL 90 residues - Formula weight is not available

1   SERSERVALGLNTHRALAALATHRSERTRP
2   GLYTHRVALPROSERILEARGVALTYRTHR
3   ALAASNASNGLYLYSILETHRGLUARGCYS
4   TRPASPGLYLYSGLYTRPTYRTHRGLYALA
5   PHEASNGLUPROGLYASPASNVALSERVAL
6   THRSERTRPLEUVALGLYSERALAILEHIS
7   ILEARGVALTYRALASERTHRGLYTHRTHR
8   THRTHRGLUTRPCYSTRPASPGLYASNGLY
9   TRPTHRLYSGLYALATYRTHRALATHRASN

Entity 2, ligand - 164.156 Da.

1   FUC

Samples:

sample_1: RSL, [U-100% 13C; U-100% 15N], 2 mM; fucose 24 mM; potassium phosphate 20 mM; sodium chloride 50 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 68 mM; pH: 6.1; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

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

CCPN, Vranken et al. - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian Uniform NMR System 800 MHz

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