BMRB Entry 15466

Name: STRUCTURE CHARACTERISATION OF PINA WW DOMAIN AND COMPARISON WITH OTHER GROUP IV WW DOMAINS, PIN1 AND ESS1
Published: 2008-06-25

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PDB ID: 2jv4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15466
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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:

STRUCTURE CHARACTERISATION OF PINA WW DOMAIN AND COMPARISON WITH OTHER GROUP IV WW DOMAINS, PIN1 AND ESS1

Deposition date:

2007-09-11

Original release date:

2008-06-25

Authors:

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

Citation:

Citation: Ng, Chai; Kato, Yusuke; Tanokura, Masaru; Brownlee, Robert. "Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1" Biochim. Biophys. Acta 1784, 1208-1214 (2008).
PubMed: 18503784

Assembly members:

Assembly members:
PEPTIDYL-PROLYL_CIS/TRANS_ISOMERASE, polymer, 54 residues, 6262.056 Da.

Natural source:

Natural source: Common Name: ASPERGILLUS NIDULANS Taxonomy ID: 162425 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: ASPERGILLUS NIDULANS

Experimental source:

Experimental source: Production method: recombinant technology Host organism: ESCHERICHIA COLI Vector: PLYSS

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PEPTIDYL-PROLYL_CIS/TRANS_ISOMERASE: GSMVNTGLPAGWEVRHSNSK NLPYYFNPATRESRWEPPAD TDMETLKMYMATYH

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	PEPTIDYL-PROLYL CIS/TRANS ISOMERASE	1

Entities:

Entity 1, PEPTIDYL-PROLYL CIS/TRANS ISOMERASE 54 residues - 6262.056 Da.

1

GLY

SER

MET

VAL

ASN

THR

GLY

LEU

PRO

ALA

2

GLY

TRP

GLU

VAL

ARG

HIS

SER

ASN

SER

LYS

3

ASN

LEU

PRO

TYR

PHE

ASN

PRO

ALA

THR

4

ARG

GLU

SER

ARG

TRP

GLU

PRO

ALA

ASP

5

THR

ASP

MET

GLU

THR

LEU

LYS

MET

TYR

MET

6

ALA

THR

TYR

HIS

Samples:

sample_1: PEPTIDYL-PROLYL CIS/TRANS ISOMERASE, [U-100% 13C; U-100% 15N], 1.8 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02%; H2O 90%; D2O 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_1	isotropic	sample_conditions_1
3D_13C- SEPARATED_ NOESY	sample_1	isotropic	sample_conditions_1
3D_15N- SEPARATED_ NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HCCH -COSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

SPARKY v3, Goddard - chemical shift assignment, data analysis, peak picking

VNMR, Varian - collection

TALOS, Cornilescu, Delaglio and Bax - Dihedral angle

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - Energy minimisation, refinement

NMR spectrometers:

VARIAN INOVA 500 MHz

BMRB	15003
PDB	2JV4
GB	AAC49984 EAA57931
REF	XP_663749
TPE	CBF70093