BMRB Entry 25976

Name: Solution structure of the HYD1 hydrophobin from Schizophyllum commune
Published: 2016-03-30

Click here to enlarge.

PDB ID: 2nbh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25976
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of the HYD1 hydrophobin from Schizophyllum commune

Deposition date:

2016-02-21

Original release date:

2016-03-30

Authors:

Langelaan, David; Smith, Steven; Grondin, Julie

Citation:

Citation: Langelaan, David; Smith, Steven; Master, Emma; Gandier, Julie-Anne; Grondin, Julie. "Structure of a fungal hydrophobin" .

Assembly members:

Assembly members:
Hydrophobin, polymer, 107 residues, 10873.522 Da.

Natural source:

Natural source: Common Name: Schizophyllum commune Taxonomy ID: 5334 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Schizophyllum commune

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 32

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Hydrophobin: KAMADIGSTAVPRDVNGGTP PKSCSSGPVYCCNKTEDSKH LDKGTTALLGLLNIKIGDLK DLVGLNCSPLSVIGVGGNSC SAQTVCCTNTYQHGLVNVGC TPINIGL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	379
15N chemical shifts	91
1H chemical shifts	574

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Hydrophobin	1

Entities:

Entity 1, Hydrophobin 107 residues - 10873.522 Da.

1

LYS

ALA

MET

ALA

ASP

ILE

GLY

SER

THR

ALA

2

VAL

PRO

ARG

ASP

VAL

ASN

GLY

THR

PRO

3

PRO

LYS

SER

CYS

SER

GLY

PRO

VAL

TYR

4

CYS

ASN

LYS

THR

GLU

ASP

SER

LYS

HIS

5

LEU

ASP

LYS

GLY

THR

ALA

LEU

GLY

6

LEU

ASN

ILE

LYS

ILE

GLY

ASP

LEU

LYS

7

ASP

LEU

VAL

GLY

LEU

ASN

CYS

SER

PRO

LEU

8

SER

VAL

ILE

GLY

VAL

GLY

ASN

SER

CYS

9

SER

ALA

GLN

THR

VAL

CYS

THR

ASN

THR

10

TYR

GLN

HIS

GLY

LEU

VAL

ASN

VAL

GLY

CYS

11

THR

PRO

ILE

ASN

ILE

GLY

LEU

Samples:

sample_1: Hydrophobin, [U-13C; U-15N], 1 mM; TRIS 25 mM; sodium chloride 150 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 8; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
1H-15N Heteronuclear NOE	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ, Varian - collection

CcpNmr_Analysis, Wim F. Vranken, Wayne Boucher, Tim J. Stevens, Rasmus H. Fogh, - chemical shift assignment

ARIA v1.3, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

Varian INOVA 600 MHz

UNP	D8QCG9_SCHCM
AlphaFold	D8QCG9