BMRB Entry 11428

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR11428

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Title:
1H, 15N chemical shift assignments for a disulfide-deficient mutant of the starch-binding domain of glucoamylase
Deposition date:
2011-02-13
Original release date:
2011-09-28
Authors:
Sugimoto, Hayuki; Noda, Yasuo; Segawa, Shin-ichi
Citation:

Citation: Sugimoto, Hayuki; Noda, Yasuo; Segawa, Shin-ichi. "NMR analysis of a kinetically trapped intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase"  J. Mol. Biol. 412, 304-315 (2011).
PubMed: 21801731

Assembly members:

Assembly members:
a disulfide-deficient mutant of the starch-binding domain of glucoamylase, polymer, 110 residues, 12100 Da.

Natural source:

Natural source:   Common Name: Aspergillus niger   Taxonomy ID: 5061   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Aspergillus niger

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
a disulfide-deficient mutant of the starch-binding domain of glucoamylase: TSGTTPTAVAVTFDLTATTT YGENIYLVGSISQLGDWETS DGIALSADKYTSSDPLWYVT VTLPAGESFEYKFIRIESDD SVEWESDPNREYTVPQAGGT STATVTDTWR

Data sets:
Data typeCount
15N chemical shifts109
1H chemical shifts616

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1a disulfide-deficient mutant of the starch-binding domain of glucoamylase1

Entities:

Entity 1, a disulfide-deficient mutant of the starch-binding domain of glucoamylase 110 residues - 12100 Da.

This molecule is a mutant protein (C3G and C98G) of the starch-binding domain of Aspergillus niger glucoamylase (residues 507-616).

1   THRSERGLYTHRTHRPROTHRALAVALALA
2   VALTHRPHEASPLEUTHRALATHRTHRTHR
3   TYRGLYGLUASNILETYRLEUVALGLYSER
4   ILESERGLNLEUGLYASPTRPGLUTHRSER
5   ASPGLYILEALALEUSERALAASPLYSTYR
6   THRSERSERASPPROLEUTRPTYRVALTHR
7   VALTHRLEUPROALAGLYGLUSERPHEGLU
8   TYRLYSPHEILEARGILEGLUSERASPASP
9   SERVALGLUTRPGLUSERASPPROASNARG
10   GLUTYRTHRVALPROGLNALAGLYGLYTHR
11   SERTHRALATHRVALTHRASPTHRTRPARG

Samples:

sample_1: a disulfide-deficient mutant of the starch-binding domain of glucoamylase, [U-99% 15N], 1 mM; sodium phosphate 20 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.08 M; pH: 7.0; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
3D 1H-15N HSQC-NOESY-HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection, processing

SPARKY v3.114, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 4011
PDB
EMBL CAA25219 CAA25303 CAK38411
GB AAB59296 AAP04499 AAT58037 AAT67041 ABV82763
PRF 1008149A
REF XP_001390530
SP P69327 P69328
AlphaFold P69327 P69328

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