BMRB Entry 17765

Name: Identification of the key regions that drive functional amyloid formation by the fungal hydrophobin EAS
Published: 2012-01-24

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PDB ID: 2lfn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17765
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Identification of the key regions that drive functional amyloid formation by the fungal hydrophobin EAS

Deposition date:

2011-07-06

Original release date:

2012-01-24

Authors:

Macindoe, Ingrid; Kwan, Ann; Morris, Vanessa; Mackay, Joel; Sunde, Margie

Citation:

Citation: Macindoe, Ingrid; Kwan, Ann; Ren, Qin; Morris, Vanessa; Yang, Wenrong; Mackay, Joel; Sunde, Margaret. "Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS." Proc. Natl. Acad. Sci. U.S.A. 109, E804-E811 (2012).
PubMed: 22308366

Assembly members:

Assembly members:
entity, polymer, 68 residues, 6728.595 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SATTIGPNTCSIDDYKPYCC QSMSGSASLGCVVGVIGSQC GASVKCCKDDVTNTGNSGLI INAANCVA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	420

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EAS	1

Entities:

Entity 1, EAS 68 residues - 6728.595 Da.

Residue 1 represents a cloning artifact.

1

SER

ALA

THR

ILE

GLY

PRO

ASN

THR

CYS

2

SER

ILE

ASP

TYR

LYS

PRO

TYR

CYS

3

GLN

SER

MET

SER

GLY

SER

ALA

SER

LEU

GLY

4

CYS

VAL

GLY

VAL

ILE

GLY

SER

GLN

CYS

5

GLY

ALA

SER

VAL

LYS

CYS

LYS

ASP

6

VAL

THR

ASN

THR

GLY

ASN

SER

GLY

LEU

ILE

7

ILE

ASN

ALA

ASN

CYS

VAL

ALA

Samples:

sample_1: EAS 890 uM; D2O 5%; H2O 95%; DSS20 – 34 uM; sodium phosphate 20 mM

sample_2: EAS, [U-98% 15N], 280 uM; D2O 5%; H2O 95%; DSS20 – 34 uM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HNHA	sample_2	isotropic	sample_conditions_2

Software:

TOPSPIN vv1.3, Bruker Biospin - collection, processing

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

ARIA vv1.2, Linge, O'Donoghue and Nilges - refinement, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

ProcheckNMR, Laskowski and MacArthur - structure validation

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

Bruker Avance 600 MHz