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- PDB-4bwh: Solution structure of the chimeric hydrophobin NChi2 -

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Basic information

Entry
Database: PDB / ID: 4bwh
TitleSolution structure of the chimeric hydrophobin NChi2
ComponentsNCHI2, HYDROPHOBIN, NCHI2
KeywordsSTRUCTURAL PROTEIN / SELF-ASSEMBLY / AMYLOID / INTERFACE / CHIMERA
Function / homology
Function and homology information


structural constituent of cell wall / fungal-type cell wall / cell wall organization / extracellular region
Similarity search - Function
Cerato-ulmin hydrophobin family / Fungal hydrophobin / Hydrophobin, conserved site / Fungal hydrophobins signature. / hfbii hydrophobin / Hydrophobin / Hydrophobin superfamily / Hydrophobin / Hydrophobins / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
Hydrophobin / Hydrophobin
Similarity search - Component
Biological speciesNEUROSPORA CRASSA (fungus)
MethodSOLUTION NMR / ARIA2
AuthorsRen, Q. / Sunde, M. / Kwan, A.H.
CitationJournal: To be Published
Title: Solution Structure of the Chimeric Hydrophobin Nchi2
Authors: Ren, Q. / Macindoe, I. / Sunde, M. / Kwan, A.
History
DepositionJul 3, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 6, 2014Provider: repository / Type: Initial release
Revision 2.0Jun 14, 2023Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Other
Category: atom_site / database_2 ...atom_site / database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _atom_site.Cartn_x / _atom_site.Cartn_y ..._atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: NCHI2, HYDROPHOBIN, NCHI2


Theoretical massNumber of molelcules
Total (without water)9,0291
Polymers9,0291
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 500LOWEST ENERGY
RepresentativeModel #1

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Components

#1: Protein NCHI2, HYDROPHOBIN, NCHI2 / RODLET PROTEIN


Mass: 9029.109 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: THE FIRST RESIDUE (S) OF THE CONSTRUCT IS A CLONING ARTEFACT. THE FIRST RESIDUE OF THE MATURE PROTEIN AFTER SIGNAL PEPTIDE CLEAVAGE (A) IS MISSING. THIS IS A CHIMERIC PROTEIN OF NC2 (UNIPROT ...Details: THE FIRST RESIDUE (S) OF THE CONSTRUCT IS A CLONING ARTEFACT. THE FIRST RESIDUE OF THE MATURE PROTEIN AFTER SIGNAL PEPTIDE CLEAVAGE (A) IS MISSING. THIS IS A CHIMERIC PROTEIN OF NC2 (UNIPROT Q7S3P5, RESIDUES 19-80 AND 91-97) AND EAS (UNIPROT Q04571, RESIDUES 88-105)
Source: (gene. exp.) NEUROSPORA CRASSA (fungus) / Strain: 4R74A, 4R74A
Description: ARTIFICIAL CHIMERIC PROTEIN, SEE DETAILS IN MOLECULE SECTION.
Plasmid: PHUE / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q7S3P5, UniProt: Q04571

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111H-H NOESY
222T1
232T2
242HETERONOE
NMR detailsText: THE STRUCTURE WAS DETERMINED USING H-H NOESY WITH UNLABELLED NCHI2 TOGETHER WITH PREDICTED TORSION ANGLE RESTRAINTS FROM 1H, 13C, AND 15N CHEMICAL SHIFTS.

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Sample preparation

Details
Solution-IDContents
190% H2O/10% D2O
290% H2O/10% D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
150.0 mM2.5 1.0 atm318.0 K
250.0 mM2.5 1.0 atm318.0 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
CNSBRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ, RICE,SIMONSON,WARRENrefinement
CcpNmr Analysis2.1structure solution
MolProbity4.02Bstructure solution
MOLMOL2K.2structure solution
DANGLE1.1structure solution
PROCHECK / PROCHECK-NMR3.4structure solution
TopSpin2.1structure solution
RefinementMethod: ARIA2 / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 500 / Conformers submitted total number: 20

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