BMRB Entry 19987

Title:
Characterization and structure of the MIT1 domain of a chitin synthase from the Oomycete Saprolegnia monoica
Deposition date:
2014-05-27
Original release date:
2015-05-26
Authors:
Bulone, Vincent; Szpryngiel, Scarlett; Brown, Christian; Ye, Weihua
Citation:

Citation: Bulone, Vincent; Maler, Lena; Brown, Christian; Szpryngiel, Scarlett; KUANG, Guanglin; SRIVASTAVA, Vaibhav; Ye, Weihua; Tu, Yaoquan. "Characterization and structure of the MIT domains of two chitin synthases from the Oomycete Saprolegnia monoica"  Biochem. J. ., .-..

Assembly members:

Assembly members:
SmChs_MIT1, polymer, 74 residues, 8527.742 Da.

Natural source:

Natural source:   Common Name: oomycetes   Taxonomy ID: 37553   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Saprolegnia monoica

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28a(+)

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts278
15N chemical shifts73
1H chemical shifts494

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SmChs MIT11

Entities:

Entity 1, SmChs MIT1 74 residues - 8527.742 Da.

1   METGLYTHRILEASPASPALAPHEARGALA
2   ILEGLUARGALAILEGLNALAGLUASNGLU
3   GLYARGTYRARGGLUALALEULYSHISPHE
4   LEUASPGLYGLYGLUMETILEVALTHRALA
5   ALAGLULYSGLUALASERGLNLYSVALARG
6   ASNLEULEULEUHISLYSGLYLYSGLUVAL
7   LEUGLUTRPALAGLUHISLEUALAGLUTRP
8   ILELEUGLUHIS

Samples:

sample_1: SmChs_MIT1, [U-100% 13C; U-100% 15N], 0.3 – 1.0 mM; D2O 10%; sodium phosphate 50 mM; sodium chloride 150 mM; H2O 90%

sample_conditions_1: ionic strength: 200 mM; pH: 5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
GB ADE62520 EQC35650 KDO24422
REF XP_008610967 XP_012204852

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