BMRB Entry 15003

Name: SOLUTION STRUCTURE OF GROUP IV WW DOMAIN: A.NIDULANS PINA
Published: 2008-02-04

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15003

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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:

SOLUTION STRUCTURE OF GROUP IV WW DOMAIN: A.NIDULANS PINA

Deposition date:

2006-10-25

Original release date:

2008-02-04

Authors:

Ng, C.; Kato, Y.; Tanokura, M.; Brownlee, R.

Citation:

Citation: Kato, Yusuke; Ng, Chai; Brownlee, Robert; Tanokura, Masaru. "PinA from Aspergillus nidulans binds to pS/pT-P motifs using the same Loop I and XP groove as mammalian Pin1." Biochim. Biophys. Acta. 1774, 1208-1212 (2007).
PubMed: 17693144

Assembly members:

Assembly members:
WW_Domain_polypeptide, polymer, 53 residues, 6205.003 Da.

Natural source:

Natural source: Common Name: Aspergillus Nidulans Taxonomy ID: 162425 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Emericella nidulans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: BL21(DE3)/pLysS

Entity Sequences (FASTA):

Entity Sequences (FASTA):
WW_Domain_polypeptide: SMVNTGLPAGWEVRHSNSKN LPYYFNPATRESRWEPPADT DMETLKMYMATYH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	145
15N chemical shifts	49
1H chemical shifts	330

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	WW Domain	1

Entities:

Entity 1, WW Domain 53 residues - 6205.003 Da.

1

SER

MET

VAL

ASN

THR

GLY

LEU

PRO

ALA

GLY

2

TRP

GLU

VAL

ARG

HIS

SER

ASN

SER

LYS

ASN

3

LEU

PRO

TYR

PHE

ASN

PRO

ALA

THR

ARG

4

GLU

SER

ARG

TRP

GLU

PRO

ALA

ASP

THR

5

ASP

MET

GLU

THR

LEU

LYS

MET

TYR

MET

ALA

6

THR

TYR

HIS

Samples:

sample: WW Domain polypeptide, [U-100% 13C; U-100% 15N], 1.8 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 5.0; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNHA	sample	isotropic	sample_conditions_1
3D_13C- SEPARATED_NOESY	sample	isotropic	sample_conditions_1
3D_15N- SEPARATED_NOESY	sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample	isotropic	sample_conditions_1
3D HNCACB	sample	isotropic	sample_conditions_1
3D HNCA	sample	isotropic	sample_conditions_1
3D HN(COCA)CB	sample	isotropic	sample_conditions_1
3D HCCH-COSY	sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample	isotropic	sample_conditions_1

Software:

CYANA v2.1, T Herrmann, P Guntert and K Wuthrich - automated peak assignments, refinement, structure solution

NMRPipe, F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax - processing

SPARKY v3, T Goddard - chemical shift assignment, data analysis

VNMR, Varian - collection

TALOS, G Cornilescu, F Delaglio and A Bax - coupling constant

NMR spectrometers:

Varian INOVA 500 MHz

BMRB	15466
PDB	2JV4
GB	AAC49984 EAA57931
REF	XP_663749
TPE	CBF70093