BMRB Entry 15863

Name: Solution structure of EAS D15 truncation mutant
Published: 2008-09-24

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PDB ID: 2k6a
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15863
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of EAS D15 truncation mutant

Deposition date:

2008-07-07

Original release date:

2008-09-24

Authors:

Kwan, Ann

Citation:

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).
PubMed: 18674544

Assembly members:

Assembly members:
EAS_D15, polymer, 68 residues, 6818.720 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):
EAS_D15: SATTIGPNTCSIDDYKPYCC QSMSGSASLGCVVGVIGSQC GASVKCCKDDVTNTGNSFLI INAANCVA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
15N chemical shifts	72
1H chemical shifts	417

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EAS_D15	1

Entities:

Entity 1, EAS_D15 68 residues - 6818.720 Da.

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

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

PHE

LEU

ILE

7

ILE

ASN

ALA

ASN

CYS

VAL

ALA

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:

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

SWS	Q04571
BMRB	17765
PDB	2K6A 2LFN