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 15863

Title: Solution structure of EAS D15 truncation mutant   PubMed: 18674544

Authors: Kwan, Ann

Citation: Kwan, Ann; Macindoe, Ingrid; Paul, Vukasin; Morris, Vanessa; Kass, Itamar; Gupte, Rima; Mark, Alan; Templeton, Matthew; Mackay, Joel; Sunde, Margaret. "The Cys3-Cys4 loop of the hydrophobin EAS is not required for rodlet formation and surface activity"  J. Mol. Biol. 382, 708-720 (2008).

Assembly members:
EAS_D15, polymer, 68 residues, 6818.720 Da.

Natural source:   Common Name: Neurospora crassa   Taxonomy ID: 5141   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Neurospora crassa

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

Entity Sequences (FASTA):
EAS_D15: SATTIGPNTCSIDDYKPYCC QSMSGSASLGCVVGVIGSQC GASVKCCKDDVTNTGNSFLI INAANCVA

Data sets:
Data typeCount
15N chemical shifts72
1H chemical shifts417

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1EAS_D151

Entities:

Entity 1, EAS_D15 68 residues - 6818.720 Da.

Residue 1 (Ser) represents a non-native residue from cloning.

1   SERALATHRTHRILEGLYPROASNTHRCYS
2   SERILEASPASPTYRLYSPROTYRCYSCYS
3   GLNSERMETSERGLYSERALASERLEUGLY
4   CYSVALVALGLYVALILEGLYSERGLNCYS
5   GLYALASERVALLYSCYSCYSLYSASPASP
6   VALTHRASNTHRGLYASNSERPHELEUILE
7   ILEASNALAALAASNCYSVALALA

Samples:

sample_1: EAS_D15 0.3-0.5 ± 0.05 mM; sodium phosphate 20 ± 2 mM

sample_2: EAS_D15, [U-99% 15N], 0.1-0.3 ± 0.05 mM; sodium acetate 20 ± 2 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

XWINNMR, Bruker Biospin - collection

SPARKY v3.113, Goddard - chemical shift assignment, chemical shift calculation, data analysis, peak picking

CNS, Linge, O'Donoghue and Nilges - structure solution

ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

SWS Q04571
BMRB 17765
PDB