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- PDB-2lsh: Solution structure of the class I hydrophobin DewA -

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Basic information

Entry
Database: PDB / ID: 2lsh
TitleSolution structure of the class I hydrophobin DewA
ComponentsSpore-wall fungal hydrophobin dewA
KeywordsPROTEIN FIBRIL / hydrophobin / functional amyloid / surface active protein
Function / homology
Function and homology information


asexual spore wall assembly / spore wall / structural constituent of cell wall / fungal-type cell wall / extracellular region
Similarity search - Function
Fungal hydrophobin / Hydrophobin, conserved site / Fungal hydrophobins signature. / Hydrophobin / Hydrophobins
Similarity search - Domain/homology
Spore-wall fungal hydrophobin dewA
Similarity search - Component
Biological speciesAspergillus nidulans (mold)
MethodSOLUTION NMR / simulated annealing, molecular dynamics
Model detailsclosest to the average, model1
AuthorsMorris, V.K. / Kwan, A.H. / Mackay, J.P. / Sunde, M.
CitationJournal: J.Mol.Biol. / Year: 2012
Title: Analysis of the structure and conformational states of DewA gives insight into the assembly of the fungal hydrophobins
Authors: Morris, V.K. / Kwan, A.H. / Sunde, M.
History
DepositionApr 30, 2012Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Nov 21, 2012Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.2Oct 30, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Spore-wall fungal hydrophobin dewA


Theoretical massNumber of molelcules
Total (without water)11,4581
Polymers11,4581
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 500structures with the lowest energy
RepresentativeModel #1closest to the average

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Components

#1: Protein Spore-wall fungal hydrophobin dewA


Mass: 11457.821 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aspergillus nidulans (mold) / Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139 / Gene: dewA, AN8006 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P52750
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1122D 1H-15N HSQC
1222D 1H-13C HSQC
1342D 1H-1H NOESY
1423D CBCA(CO)NH
1523D C(CO)NH
1623D HNCO
1723D HN(CA)CB
1823D HBHA(CO)NH
1923D HN(CA)CO
11013D 1H-15N NOESY
11113D 1H-15N TOCSY
21233D 1H-13C NOESY aliphatic
21333D (H)CCH-TOCSY

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Sample preparation

Details
Solution-IDContentsSolvent system
1300-500 uM [U-99% 15N] DewA-1, 0.1 mM DSS-2, 20 mM sodium acetate-3, 95 % H20-4, 5 % D20-5, 95% H2O/5% D2O95% H2O/5% D2O
2300-500 uM [U-98% 13C; U-98% 15N] DewA-6, 0.1 mM DSS-7, 20 mM sodium acetate-8, 95 % H20-9, 5 % D20-10, 95% H2O/5% D2O95% H2O/5% D2O
3300-500 uM [U-98% 13C; U-98% 15N] DewA-11, 0.1 mM DSS-12, 20 mM sodium acetate-13, 95 % H20-14, 5 % D20-15, 100% D2O100% D2O
4300-500 uM [U-98% 13C; U-98% 15N] DewA-16, 0.1 mM DSS-17, 20 mM sodium acetate-18, 95 % H20-19, 5 % D20-20, 95% H2O/5% D2O95% H2O/5% D2O
Sample
Conc. (mg/ml)UnitsComponentIsotopic labelingConc. range (mg/ml)Solution-ID
uMDewA-1[U-99% 15N]300-5001
0.1 mMDSS-21
20 mMsodium acetate-31
95 %H20-41
5 %D20-51
uMDewA-6[U-98% 13C; U-98% 15N]300-5002
0.1 mMDSS-72
20 mMsodium acetate-82
95 %H20-92
5 %D20-102
uMDewA-11[U-98% 13C; U-98% 15N]300-5003
0.1 mMDSS-123
20 mMsodium acetate-133
95 %H20-143
5 %D20-153
uMDewA-16[U-98% 13C; U-98% 15N]300-5004
0.1 mMDSS-174
20 mMsodium acetate-184
95 %H20-194
5 %D20-204
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
1405.51 atm298 K
2405.11 atm298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE8001
Bruker AvanceBrukerAVANCE6002

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Processing

NMR software
NameVersionDeveloperClassification
TopSpinBruker Biospincollection
TopSpinBruker Biospinprocessing
SparkyGoddardpeak picking
SparkyGoddardchemical shift assignment
TALOSCornilescu, Delaglio and Baxdata analysis
ARIA1.2Linge, O'Donoghue and Nilgesstructure solution
ARIArefinement
RefinementMethod: simulated annealing, molecular dynamics / Software ordinal: 1
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 500 / Conformers submitted total number: 20 / Representative conformer: 8

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