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 19553

Title: NMR solution structure of chitin-binding domain from dust mite group XII allergen Blo t 12.

Authors: Naik, Mandar; Kung, Camy; Huang, Tai-huang

Citation: Naik, Mandar; Kung, Camy; Huang, Tai-huang. "Solution structure of Blo 1 12 CBD domain."  Not known ., .-..

Assembly members:
entity, polymer, 69 residues, 7528.702 Da.

Natural source:   Common Name: Storage mite   Taxonomy ID: 40697   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Blomia tropicalis

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

Entity Sequences (FASTA):
entity: GPLGSDLIVHEGGKTYHVVC HEEGPIPHPGNVHKYIICSK SGSLWYITVMPCSIGTKFDP ISRNCVLDN

Data sets:
  • assigned_chemical_shifts
Data typeCount
13C chemical shifts292
15N chemical shifts66
1H chemical shifts468

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Blo 1 12 CBD domain1

Entities:

Entity 1, Blo 1 12 CBD domain 69 residues - 7528.702 Da.

Residue 75 to 79 are non-native leftover of purification tag.

1   GLYPROLEUGLYSERASPLEUILEVALHIS
2   GLUGLYGLYLYSTHRTYRHISVALVALCYS
3   HISGLUGLUGLYPROILEPROHISPROGLY
4   ASNVALHISLYSTYRILEILECYSSERLYS
5   SERGLYSERLEUTRPTYRILETHRVALMET
6   PROCYSSERILEGLYTHRLYSPHEASPPRO
7   ILESERARGASNCYSVALLEUASPASN

Samples:

CN: Blo t 12 CBD, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; potassium phosphate 50 ± 1 mM; sodium chloride 100 ± 1 mM; H2O 90 ± 1 %; D2O 10 ± 1 %

N: Blo t 12 CBD, [U-100% 15N], 1 ± 0.05 mM; potassium phosphate 50 ± 1 mM; sodium chloride 100 ± 1 mM; H2O 90 ± 1 %; D2O 10 ± 1 %

Phage: Blo t 12 CBD, [U-100% 15N], 1 ± 0.05 mM; potassium phosphate 50 ± 1 mM; sodium chloride 100 ± 1 mM; Pf1 phage 11 ± 0.1 mg/ml; H2O 90 ± 0.1 %; D2O 10 ± 0.1 %

Default: pH: 6.0; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNisotropicDefault
2D 1H-13C HSQCCNisotropicDefault
3D HNCOCNisotropicDefault
3D HNCACNisotropicDefault
3D HNCACBCNisotropicDefault
3D CBCA(CO)NHCNisotropicDefault
3D HccoNHCNisotropicDefault
3D CCcoNHCNisotropicDefault
3D HCCH-COSYCNisotropicDefault
3D HBHAcoNHCNisotropicDefault
2D-hbCBcgcdHDCNisotropicDefault
3D 1H-13C NOESYHSQCCNisotropicDefault
3D 1H-15N NOESYHSQCCNisotropicDefault
2D 1H-15N IPAP HSQCPhageanisotropicDefault

Software:

TOPSPIN v3.0, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, peak picking

CYANA v3.9, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

PSVS v1.5, Bhattacharya and Montelione - validation

X-PLOR NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAQ55550